Seattle-based biotech startup Icosavax today scored $51 million in funding to create vaccines from artificial viruses. The Series A financing was led by Qiming Venture Partners USA along with Adams Street Partners, Sanofi Ventures and NanoDimension.  [Qiming is a Chinese venture capital firm : https://en.wikipedia.org/wiki/Qiming_Venture_Partners ]

Most vaccines train the body to protect against disease using biological agents — often using a harmless form of the disease they want to protect against.

Icosavax, a University of Washington spinout, is approaching the problem a bit differently. The startup is creating virus-like particles (VLPs) that are designed on computers with technology licensed from the Institute for Protein Design (IPD) at the UW.

“[VLPs] look and smell like viruses, which is why you get this big activity of the immune system. But they’re safe because they’re not viruses,” Icosavax CEO Adam Simpson told GeekWire. The particles are currently used in approved vaccines for HPV and Hepatitis B.

Icosavax’s first goal is to create a vaccine for the respiratory syncytial virus (RSV) in adults and pursue clinical studies. In the future, they plan to use the same technology against other viruses as well.  [...]

Icosavax is the latest company to spin out of IPD, which is led by Professor David Baker. The institute won $45 million earlier this year from TED’s Audacious Project and is responsible for launching startups Arzeda, Cyrus Biotechnology, PvP Biologics, Virvio, Neoleukin Therapeutics and A-Alpha Bio.

“What they’re doing at IPD is scientifically incredible,” said Simpson, who also serves as CEO of PvP Biologics, which is working on a drug for Celiac disease.

The VLP technology was invented by IPD researcher Dr. Neil King, who serves as chair of the company’s scientific advisory board. The company’s board of directors is led by Tadataka (Tachi) Yamada, former chief medical and scientific officer of Takeda Pharmaceuticals.

Normally, it would be difficult to create a VLP for a virus-like RSV because of the complexity involved. Icosavax got around that problem with the help of proteins they designed using computers.

By building proteins from scratch, the team was able to break down the complex biological problem into more manageable parts. When combined, those parts come together to form the VLP.

“We were extremely impressed with this novel approach using computational protein design to create VLP-based vaccines that have improved efficacy and are simple to manufacture,” Mark McDade, managing partner at Qiming, said in a statement.

Icosavax’s board of directors also includes Simpson, McDade, Adams Street partner Terry Gould, U.S. head of investments at Sanofi Ventures Jason Hafler, and NanoDimension partner Eric Moessinger.

Former Takeda executive Dr. Doug Holtzman is Icosavax’s chief scientific officer, and former GSK Vaccines executive Dr. Niranjan Kanesa-thasan is chief medical officer.

[Note - Takeda is a Japan pharma co. - https://en.wikipedia.org/wiki/Takeda_Pharmaceutical_Company ] 

These diagrams show the protein structure for the “spike” that’s used by the coronavirus known as COVID-19 to force its way into cells. The diagram at left shows the spike with a molecular key known as the RBD in the “down” position. The middle diagram shows the RBD-up conformation, and the diagram at right shows the spike on the SARS virus for comparison’s sake. (Wrapp, Wang et al. / UT-Austin / NIH via Science / AAAS)

Biochemists have created the first 3-D, atomic-scale map of key proteins in the killer coronavirus, opening up new possibilities for developing treatments and a vaccine.

Researchers at the University of Washington and its Institute for Protein Design are among the sleuths who’ll be taking advantage of the new clues.

The map shows the 3-D arrangement of proteins in the molecular “spike” that the virus known as COVID-19 uses to force its way into the cells that it infects. Once the virus gains entry, it delivers genetic code that takes control of the cells to spread the infection.

[...]

Governments around the world have been using quarantines to reduce the spread of the virus, and health officials are using the best virus-fighting treatments they have on hand. But longer-term, researchers are racing to develop vaccines and other types of antiviral treatments that are specific to COVID-19. That’s where the 3-D map, published today by the journal Science, comes into play.

UW’s Institute for Protein Design has been at the forefront of protein engineering to fight disease. The institute’s technique looks at the 3-D structure of proteins, and then creates molecular “locks” and “keys” that fit onto those proteins — either to facilitate a molecular interaction or gum up the works and head off an interaction.

For COVID-19, the institute is looking for ways to gum up the works.

Researchers at the institute has already reported some success in developing a “Flu Glue” that binds itself to a protein on the outer coat of an influenza virus known as hemagglutinin or influenza HA. The newly released map could help them create similar mini-proteins for COVID-19.

Institute director David Baker said the authors of the Science study have already emailed him the coordinates for the COVID-19 map.

“We are using them to design stable mini-protein binders to different sites on the spike protein, in collaboration with David Veesler here who is providing the protein and expertise,” Baker told GeekWire in an email. “By analogy with the mini-proteins we’ve designed against influenza HA, we expect (hope) high-affinity designs to neutralize the virus.”

If the binders work the way they do with the flu virus, they could be part of an effective virus-blocking treatment, or serve as the basis for new diagnostic tools.

Veesler and his teammates at UW [see https://www.veeslerlab.com/ ] are also among many researchers around the world who are working to develop a COVID-19 vaccine.

The vaccine hunters also include the researchers at the University of Texas at Austin and the National Institutes of Health who came up with the 3-D protein map for COVID-19. They drew upon their previous experience in locking down and mapping spike proteins for other coronaviruses, such as SARS and MERS.

“As soon as we knew this was a coronavirus, we felt we had to jump at it, because we could be one of the first ones to get this structure,” UT-Austin’s Jason McLellan, the senior author of the Science study, said in a news release. “We knew exactly what mutations to put into this, because we’ve already shown these mutations work for a bunch of other coronaviruses.”

Researchers Jason McLellan and Daniel Wrapp work in the McLellan Lab at the University of Texas at Austin. (UT-Austin Photo / Vivian Abagiu)

The bulk of the research was done by the study’s principal authors, Daniel Wrapp and Nianshuang Wang of UT-Austin. Just two weeks after receiving the genome sequence of the virus from Chinese researchers, the team designed and produced samples of their stabilized spike protein. It took another 12 days to reconstruct the 3-D protein map and send the research to Science.

One of the key technologies behind the effort is cryogenic electron microscopy, or cryo-EM, which makes it possible to produce 3-D models of cellular structures, molecules and viruses. UT-Austin has a state-of-the-art cryo-EM facility at its Sauer Structural Biology Laboratory.

“We ended up being the first ones in part due to the infrastructure at the Sauer Lab,” McLellan said. “It highlights the importance of funding basic research facilities.”

In addition to facilitating the development of vaccines and synthetic antiviral mini-proteins, the 3-D map could help researchers come up with ways to isolate naturally occurring antibodies from COVID-19 patients who survive the disease. Like the mini-proteins, those antibodies could be used to treat an infection soon after exposure.

Authors of the study published by Science, “Cryo-EM Structure of the 2019-nCoV Spike in the Prefusion Conformation,” [received Feb 10 2020, accepted Feb 17 2020 - see https://www.science.org/doi/epdf/10.1126/science.abb2507 ]  include Wrapp, Wang and McLellan as well as Kizzmekia Corbett, Jory Goldsmith, Ching-Lin Hsieh, Olubukola Abiona and Barney Graham.

Seven months into the coronavirus crisis, with more than 30 vaccines rapidly advancing through the rigorous stages of clinical trials, a surprising number of research groups are placing bets on some that have not yet been given to a single person.

The New York Times has confirmed that at least 88 candidates are under active preclinical investigation in laboratories across the world, with 67 of them slated to begin clinical trials before the end of 2021.

Those trials may begin after millions of people have already received the first wave of vaccines. It will take months to see if any of them are safe and effective. Nevertheless, the scientists developing them say their designs may be able to prompt more powerful immune responses, or be much cheaper to produce, or both — making them the slow and steady winners of the race against the coronavirus.

“The first vaccines may not be the most effective,” said Ted Ross, the director of the Center for Vaccines and Immunology at the University of Georgia, who is working on an experimental vaccine he hopes to put into clinical trials in 2021.

Many of the vaccines at the front of the pack today try to teach the body the same basic lesson. They deliver a protein that covers the surface of the coronavirus, called spike, which appears to prompt the immune system to make antibodies to fight it off.

But some researchers worry that we may be pinning too many hopes on a strategy that has not been proved to work. “It would be a shame to put all our eggs in the same basket,” said [Dr. David J. Veesler (born 1981)], a virologist at the University of Washington.

In March, Dr. Veesler and his colleagues designed a vaccine that consists of millions of nanoparticles, each one studded with 60 copies of the tip of the spike protein, rather than the entire thing. The researchers thought these bundles of tips might pack a stronger immunological punch.

When the researchers injected these nanoparticles into mice, the animals responded with a flood of antibodies to the coronavirus — much more than produced by a vaccine containing the entire spike. When the scientists exposed vaccinated mice to the coronavirus, they found that it completely protected them from infection.

The researchers shared their initial results this month in a paper that has yet to be published in a scientific journal. Icosavax, a start-up company co-founded by [Dr. David J. Veesler (born 1981)]'s collaborator, Neil King, is preparing to begin clinical trials of the nanoparticle vaccine by the end of this year.

U.S. Army researchers at the Walter Reed Army Institute have created another spike-tip nanoparticle vaccine, and are recruiting volunteers for a clinical trial that they also plan to start by the end of 2020. A number of other companies and universities are creating spike-tip-based vaccines as well, using recipes of their own.

Immune punch

Antibodies are only one weapon in the immune arsenal. Blood cells known as T cells can fight infections by attacking other cells that have been infiltrated by the virus.

“We still don’t know which kind of immune response will be important for protection,” said Luciana Leite, a vaccine researcher at Instituto Butantan in São Paulo, Brazil.

It’s possible that vaccines that arouse only antibody responses will fail in the long run. Dr. Leite and other researchers are testing vaccines made of several parts of the coronavirus to see if they can coax T cells to fight it off.

“It’s a second line of defense that might work better than antibodies,” said [Dr. Anne Searls De Groot (born 1956)], the C.E.O. of [EpiVax], a company based in Providence, R.I.

Epivax has created an experimental vaccine with several pieces of the spike protein, as well as other viral proteins, which it plans to test in a clinical trial in December.

The effectiveness of a vaccine can also be influenced by how it gets into our body. All of the first-wave vaccines now in clinical trials have to be injected into muscle. A nasal spray vaccine — similar to FluMist for influenza — might work better, since the coronavirus invades our bodies through the airway.

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Several groups are gearing up for clinical trials of nasal spray vaccines. One of the most imaginative approaches comes from a New York company called Codagenix. They are testing a vaccine that contains a synthetic version of the coronavirus that they made from scratch.

The Codagenix vaccine is a new twist on an old formula. For decades, vaccine makers have created vaccines for diseases such as chickenpox and yellow fever from live but weakened viruses. Traditionally, scientists have weakened the viruses by growing them in cells of chickens or some other animal. The viruses adapt to their new host, and in the process they become ill-suited for growing in the human body.

The viruses still slip into cells, but they replicate at a glacial pace. As a result, they can’t make us sick. But a small dose of these weakened viruses can deliver a powerful jolt to the immune system.

Yet there are relatively few live weakened viruses, because making them is a struggle. “It’s really trial-and-error based,” said J. Robert Coleman, the chief executive of Codagenix. “You can never say exactly what the mutations are doing.”

The Codagenix scientists came up with a different approach. They sat down at a computer and edited the coronavirus’s genome, creating 283 mutations. They then created a piece of DNA containing their new genome and put it in monkey cells. The cells then made their rewritten viruses. In experiments on hamsters, the researchers found that their vaccine didn’t make the animals sick — but did protect them against the coronavirus.

Codagenix is preparing to open a Phase 1 trial of an intranasal spray with one of these synthesized coronaviruses as early as September. Two similar vaccines are in earlier stages of development.

The French vaccine maker Valneva plans to start clinical trials in November on a far less futuristic design. “We are addressing the pandemic with a rather conventional approach,” said Thomas Lingelbach, the C.E.O. of Valneva.

Valneva makes vaccines from inactivated viruses that are killed with chemicals. Jonas Salk and other early vaccine makers found this recipe to work well. Chinese vaccine makers already have three such coronavirus vaccines in Phase 3 trials, but Dr. Lingelbach still sees an opportunity for Valneva making its own. Inactivated virus vaccines have to meet very high standards for purification, to make sure all the viruses are not viable. Valneva has already met those standards, and it’s not clear if Chinese vaccines would.

The United Kingdom has arranged to purchase 60 million doses of Valneva’s vaccine, and the company is scaling up to make 200 million doses a year.

Faster and cheaper production

Even if the first wave of vaccines work, many researchers worry that it won’t be possible to make enough of them fast enough to tackle the global need.

“It’s a numbers game — we need a lot of doses,” said Florian Krammer, a virologist at Icahn School of Medicine at Mount Sinai in New York City.

Some of the most promising first-wave products, such as RNA vaccines from Moderna and Pfizer, are based on designs that have never been put into large-scale production before. “The manufacturing math just doesn’t add up,” said Steffen Mueller, the chief scientific officer of Codagenix.

Many of the second-wave vaccines wouldn’t require a large scale-up of experimental manufacturing. Instead, they could piggyback on standard methods that have been used for years to make safe and effective vaccines.

Codagenix, for example, has entered into a partnership with the Serum Institute of India to grow their recoded coronaviruses. The institute already makes billions of doses of live weakened virus vaccines for measles, rotaviruses and influenza, growing them in large tanks of cells.

Tapping into well-established methods could also cut down the cost of a coronavirus vaccine, which will make it easier to get it distributed to less wealthy countries.

Researchers at Baylor College of Medicine, for example, are doing preclinical work on a vaccine that they said might cost as little as $2 a dose. By contrast, Pfizer is charging $19 a dose in a deal with the U.S. government, and other companies have floated even higher prices.

To make the vaccine, the Baylor team engineered yeast to make coronavirus spike tips. It’s precisely the same method that has been used since the 1980s to make vaccines for hepatitis B. The Indian vaccine maker Biological E has licensed Baylor’s vaccine and is planning Phase 1 trials that will start this fall.

“They now already know they can make a billion doses a year,” said Maria Elena Bottazzi, a Baylor virologist. “It’s easy-breezy for them, because it was exactly the same bread-and-butter vaccine technology that they have been working with for years.”

Even if the world gets cheap, effective vaccines against Covid-19, that doesn’t mean all of our pandemic worries are over. With an abundance of other coronaviruses lurking in wild animals, another Covid-like pandemic may be not far off. Several companies — including Anhui Zhifei in China, Osivax in France and VBI in Massachusetts — are developing “universal” coronavirus vaccines that might protect people from an array of the viruses, even those that haven’t colonized our species yet.

Many scientists see their ongoing vaccine work as part of a long game — one that the well-being of entire nations will depend on. Thailand, for example, is preparing to purchase Covid-19 vaccines developed overseas, but scientists there are also carrying out preclinical research of their own.

At Chulalongkorn University, researchers have been investigating several potential candidates, including an RNA-based vaccine that will go into Phase 1 studies by early 2021. The vaccine is similar to one that Pfizer is now testing in late-stage clinical trials, but these scientists want the security of making their own version.

“While Thailand has to plan for buying vaccines, we should do our best to produce our own vaccine as well,” said Kiat Ruxrungtham, a professor at Chulalongkorn University. “If we are not successful this time, we will be capable to do much, much better in the next pandemic.”

Less isolation from family and friends. Uninterrupted education for our children. Lifesaving vaccines quickly made available to everyone around the globe.

A vision so different from what we are experiencing during the COVID-19 pandemic.

We can make it happen. But we need universal vaccines that can protect us from entire families of viruses. And we need faster vaccine development when the next novel virus emerges.

Researchers at the UW Medicine Institute for Protein Design (IPD) have made impressive breakthroughs using computer-designed synthetic proteins to develop innovative vaccines. Their work is bringing us closer to a better, safer future for everyone — but philanthropic support is critical to maintaining the momentum, so we can stop the next pandemic before it starts.

 UNIVERSAL FLU VACCINE OFFERS BROAD PROTECTION

Long before COVID-19, the influenza virus caused deadly global pandemics that killed tens of millions of people worldwide. Currently, our best defense is a seasonal flu vaccine, updated each year to protect against the three or four flu viruses that researchers believe are most likely to spread during the upcoming flu season.

But what if there was a universal flu vaccine that protected us against every type of flu virus?

“We really want to get to the point where we’re preventing the next pandemic, not responding to it. And the only way to do that is through broadly protective vaccines,” says Neil King, PhD, a biochemist at the IPD.

In 2019, an IPD group led by King, an assistant professor of biochemistry at the University of Washington School of Medicine, began developing a new vaccine to fight multiple flu viruses within the same family. By showing the immune system that different flu viruses share some of the same features, they hoped to teach the immune system to recognize and attack all viruses with this common weakness.

To create their vaccine, Dan Ellis, PhD ’21, a research scientist at the IPD, in collaboration with the National Institutes of Health, attached proteins in a repeating “mosaic” pattern on a custom-designed synthetic nanoparticle — a tiny protein particle that triggers an immune system response.

Why is the mosaic approach better? Current mRNA (messenger RNA) COVID-19 vaccines, such as Pfizer’s and Moderna’s, instruct your cells to build a harmless piece of the virus called the spike protein. Your immune system then learns to recognize that spike protein — the part that lets the virus enter and infect your cells — and attack it. But on its own, this spike protein doesn’t look like a natural virus, so it can be hard for your immune system to recognize.

By contrast, a nanoparticle vaccine can be designed with dozens of distinct proteins waving at your immune system like a series of unmistakable little flags. It’s a much more effective way to grab the immune system’s attention, so less vaccine is needed for a strong response.

Currently, Flu-Mos-v1, the IPD’s universal flu vaccine candidate, is in Phase 1 clinical trials; so far in animal testing, it has yielded a stronger immune response than seasonal vaccines. And, unlike seasonal vaccines, it’s even providing strong protection against flu viruses that weren’t part of the vaccine formula.

Ellis and his colleagues envision taking their nanoparticle approach even further in the future, using protein design to build vaccine prototypes for virus families with the greatest pandemic potential. Dr. Anthony Fauci, director of the National Institute of Allergy and Infectious Diseases, recently proposed a new federal government program to develop vaccine prototypes for 20 virus families, which could start as early as 2022.

But the IPD’s flu vaccine efforts have already helped to create another new vaccine. When COVID-19 emerged in early 2020, the King lab — along with a network of collaborators — was ready to bring their nanoparticle approach to fight the coronavirus.

Pictures of : Neil King, PhD  /  Dan Ellis, PhD ’21  /  Lexi Walls, PhD ’19

FAST-TRACKING VACCINES FOR NOVEL VIRUSES

When Lexi Walls, PhD ’19, a research scientist in the Department of Biochemistry at the University of Washington School of Medicine, began studying coronavirus spikes in 2015, not much was known about them. If scientists didn’t understand the spike’s structure, Walls realized, it would be difficult to treat or develop vaccines for that family of viruses.

As Walls completed her doctorate in December 2019, the SARS-CoV-2 virus (which causes COVID-19) was just emerging in Wuhan, China. Soon, COVID-19 was spreading rapidly around the world, and Walls’ research on the coronavirus’s spike protein would become an important part of the global response.

When the genetic sequences for the novel coronavirus were released in January 2020, Walls and her advisor, David Veesler, PhD, an associate professor of biochemistry at the University of Washington School of Medicine, immediately reached out to King to propose a collaboration.

“Neil jumped on board right away, and he got a huge team of people at the IPD to join forces quickly,” says Walls. “We were constantly talking, sharing data and helping each other solve problems. I had never had a collaboration like that before, and it was really fun to be working towards the same goal with the same intensity at the same time.”

The collaborators adapted the King group’s nanoparticle design to create a new COVID-19 vaccine candidate, named RBD-I53-50. Unlike mRNA vaccines, RBD-I53-50 is shelf-stable, so it’s easier to store and doesn’t need refrigeration, an important factor for global distribution. RBD-I53-50 focuses on the Achilles’ heel of the SARS-CoV-2 spike protein, called the receptor-binding domain, driving the immune system to block entry of the virus into our cells.

With funding from the Bill & Melinda Gates Foundation and the Coalition for Epidemic Preparedness Innovations (CEPI), the Veesler and King labs teamed up with the IPD spinout company Icosavax and SK bioscience, based in South Korea, to develop the vaccine. In late 2020, SK bioscience began a combined Phase 1/2 clinical study, which is currently in the second stage. And in August 2021, they received support for a Phase 3 study, bringing the vaccine another step closer to approval and distribution.

Although the RBD-I53-50 vaccine is advancing quickly, Ellis emphasizes that years of scientific research laid the foundation for its development.

“The trajectory of vaccine research isn’t always straight,” says Ellis. “But even if research doesn’t lead to a successful vaccine for one virus, it can enable very important developments for other viruses. For example, even though we don’t yet have a successful HIV vaccine, that research has made many other vaccines possible, including for COVID-19. So preparing for as many pandemic threats as possible will advance science and the future of vaccines.”

And the IPD’s long-term vision is even more ambitious. They want to significantly expand the computing power of their protein-design software so new vaccine candidates like RBD-I53-50 can be developed and made ready for testing in just weeks.

Today, we’re still facing COVID-19. But it’s only a matter of time until the next viral threat emerges. So how can we get closer to a pandemic-free tomorrow?

 YOUR SUPPORT BUILDS A BRIGHTER FUTURE

Throughout the pandemic, philanthropic support has been critical in empowering the IPD’s rapid response. Their groundbreaking work on nanoparticle vaccines was supported by the Bill & Melinda Gates Foundation, the National Institutes of Health, and gifts from Open Philanthropy, The Audacious Project, Jodi Green and Mike Halperin, Nicolas and Leslie Hanauer, anonymous donors and other granting agencies.

“The role of philanthropy in catalyzing the protein design revolution can’t be overstated,” says King. “It’s been absolutely essential, allowing us to seize the moment by providing flexible funding that we can direct to the most important problems of the day. When SARS-CoV-2 hit, philanthropic support enabled us to immediately pivot and attack this problem with everything we had.”

Soon, the IPD’s work will receive additional funding. David Baker, PhD, director of the IPD, is the 2021 recipient of the Breakthrough Prize in Life Sciences, which recognizes the world’s top scientists working in the fundamental sciences. This prestigious award includes a $3 million prize, the full amount of which Baker is donating to the IPD. Baker’s gift — which was matched generously by friends of the IPD — establishes the Breakthrough Fund at Seattle Foundation, which solely supports the IPD to advance the rapidly developing field of protein design.

But ongoing support will be needed to keep advancing the IPD’s bold mission.

Now, let’s imagine a brighter future. Universal vaccines could protect us from all strains of flu or SARS-CoV-2. The next time a new viral threat begins to spread, we could have vaccine prototypes already stockpiled, allowing us to develop vaccine candidates in a matter of weeks. No one would ever have to endure a global pandemic like COVID-19 again. And, with the help of philanthropic support, protein design can make it all possible.

• Clinical testing found the vaccine outperforms Oxford/AstraZeneca’s

• The protein-based vaccine, now called SKYCovione, does not require deep freezing

• University of Washington to waive royalty fees for the duration of the pandemic

• South Korea to purchase 10 million doses for domestic use

A vaccine for COVID-19 developed at the University of Washington School of Medicine has been approved by the Korean Ministry of Food and Drug Safety for use in individuals 18 years of age and older. The vaccine, now known as SKYCovione, was found to be more effective than the Oxford/AstraZeneca vaccine sold under the brand names Covishield and Vaxzevria.

SK bioscience, the company leading the SKYCovione’s clinical development abroad, is now seeking approval for its use in the United Kingdom and beyond. If approved by the World Health Organization, the vaccine will be made available through COVAX, an international effort to equitably distribute COVID-19 vaccines around the world. In addition, the South Korean government has agreed to purchase 10 million doses for domestic use.

The Seattle scientists behind the new vaccine sought to create a ‘second-generation’ COVID-19 vaccine that is safe, effective at low doses, simple to manufacture, and stable without deep freezing. These attributes could enable vaccination at a global scale by reaching people in areas where medical, transportation, and storage resources are limited.

“We know more than two billion people worldwide have not received a single dose of vaccine,” said David Veesler, associate professor of biochemistry at UW School of Medicine and co-developer of the vaccine. “If our vaccine is distributed through COVAX, it will allow it to reach people who need access.”

The University of Washington is licensing the vaccine technology royalty-free for the duration of the pandemic.

Clinical trial results

A multinational Phase 3 trial involving 4,037 adults over 18 years of age found that the vaccine, now called SKYCovione, elicits roughly three times more neutralizing antibodies than the Oxford/AstraZeneca vaccine Covishield/Vaxzevria. In these studies, SKYCovione or Covishield/Vaxzevria was administered twice with an interval of four weeks.

In addition, the ‘antibody conversion rate’, which refers to the proportion of subjects whose virus-neutralizing antibody level increased fourfold or more after vaccination, was higher with SKYCovione. According to data collected by SK bioscience, 98 percent of subjects achieved antibody conversion, compared to 87 percent for the control vaccine.

Among study participants 65 years of age or older, the antibody conversion rate of those vaccinated with SKYCovione was over 95 percent, which was a significant difference compared to the control vaccine (about 79 percent for the elderly), raising the expectation that SKYCovione can be used effectively to protect the elderly.

The Phase 3 trial also found that T cell activation levels, which help protect the body from COVID-19, were similar or higher with SKYCovione.

Phase 1/2 trial results announced by SK bioscience last November and posted as a preprint found that SKYCovione was safe and produced virus-neutralizing antibodies in all trial participants receiving the adjuvanted vaccine. In the Phase 3 trial, there were again no serious adverse reactions to the vaccine.

How the vaccine works

Unlike the earliest approved vaccines for COVID-19 that make use of mRNA, viral vectors, or an inactivated virus, SKYCovione is made of proteins that form tiny particles studded with fragments of the pandemic coronavirus. These nanoparticles were designed by scientists at UW Medicine and advanced into clinical trials by SK bioscience and GlaxoSmithKline with financial support from the Coalition for Epidemic Preparedness Innovations. SKYCovione includes GlaxoSmithKline’s pandemic adjuvant, AS03.

“This vaccine was designed at the molecular level to present the immune system with a key part of the coronavirus spike protein. We know this part, called the receptor-binding domain, is targeted by the most potent antibodies,” said Neil King, an assistant professor of biochemistry at UW Medicine and co-developer of the vaccine.

Two laboratories in the UW Medicine Department of Biochemistry led the initial development of the protein-based vaccine: the King Lab pioneered the vaccine’s self-assembling protein nanoparticle technology while the Veesler Lab identified and integrated a key fragment of the SARS-CoV-2 Spike protein onto the nanoparticles.

Years in the making

David Veesler, an assistant professor and HHMI investigator at UW Medicine, has been studying coronaviruses since 2015. Using advanced electron microscopes, researchers in the Veesler lab were the first to identify how the novel coronavirus enters human cells. They were also among the first to report, in Cell, detailed structural information about the virus’ spike protein, a critical piece of its infectious machinery.

In 2016, scientists in the King lab at the UW Medicine Institute for Protein Design began developing a strategy for building a new type of vaccine. They designed proteins that self-assemble into precise spherical particles and later showed that these nanoparticles could be decorated with proteins from a virus. 

Researchers from the two labs worked together in the earliest months of the COVID-19 pandemic to design a protein nanoparticle decorated with 60 copies of the Spike protein receptor-binding domain. The designed nanostructure mimics the repetitive nature of proteins on the surface of viruses, a property that the immune system responds strongly to.

“In order to focus the antibody response where it matters most, we decided to include in the vaccine only a key fragment of the coronavirus spike protein, known as the receptor-binding domain,” said Veesler. “We are thrilled to see that this strategy paid off and has led to a successful subunit vaccine.”

In initial animal studies reported in late 2020 in Cell, the nanoparticle vaccine was found to produce high levels of virus-neutralizing antibodies at low doses. These antibodies target several different sites on the coronavirus Spike protein, a desirable quality that may enhance protection against future coronavirus variants. 

Further preclinical studies, published in Nature, also showed that the vaccine conferred robust protection and produced a strong B-cell response in non-human primates, which may improve how long the protective effects of the vaccine last

In a recent preprint, a third dose of the vaccine was found to confer strong protection against the Omicon variant of COVID-19 in animals. SK bioscience will initiate testing third doses in 750 human adults soon.

The role of philanthropy

Development of the vaccine at UW Medicine was supported by the Bill & Melinda Gates Foundation, National Institutes of Health, Pew Charitable Trust, Burroughs Wellcome Fund, Fast Grants, and by gifts from Jodi Green and Mike Halperin, Nicolas and Leslie Hanauer, Rob Granieri, anonymous donors, and other granting agencies, including Open Philanthropy. Support leveraged via The Audacious Project was made possible through the generosity of Laura and John Arnold, Steve and Genevieve Jurvetson, Chris Larsen and Lyna Lam, Lyda Hill Philanthropies, Miguel McKelvey, the Clara Wu and Joe Tsai Foundation, Rosamund Zander and Hansjörg Wyss for the Wyss Foundation, and several anonymous donors.

SK bioscience received support for clinical testing from the Bill & Melinda Gates Foundation and the Center for Epidemic Preparedness (CEPI), which is a global partnership supporting vaccine development to fight pandemics. CEPI, along with the World Health Organization and Gavi, the Vaccine Alliance, are co-leaders of COVAX.

A COVID-19 vaccine developed by UW Medicine researchers has been approved in Korea, becoming the first COVID therapeutic technology from the Seattle health care system to be greenlighted for patient use.

UW Medicine scientists who worked on the technology behind the vaccine say their version is a “second-generation” COVID immunization that’s protein-based — different from the mRNA vaccines developed by Pfizer and Moderna. As a result, the vaccine, trademarked as SKYCovione, is effective in low doses, simple to manufacture and stable without deep freezing, said Neil King and David Veesler, both UW Medicine biochemistry professors and vaccine co-developers.

“We had already been working together before the pandemic, but when the pandemic hit, it was just this immediate, ‘Let’s do this’ joining of the forces between our two groups, which was really fun and highly productive,” King said.

The vaccine, which was approved for patient use by the Korean Ministry of Food and Drug Safety last week, is now pursuing authorization in the U.K. and other countries, according to a UW Medicine statement. If the vaccine is approved for emergency use by the World Health Organization, it will become available through COVAX, an international effort to distribute vaccines equitably around the world.

UW Medicine is licensing the vaccine technology royalty-free for as long as the pandemic lasts, the statement said. Several donors, including the Bill & Melinda Gates Foundation, National Institutes of Health and Pew Charitable Trust, among others, also helped fund the vaccine development.

It’s unclear whether the team will pursue U.S. Food and Drug Administration licensure in the future, instead focusing on getting shots to more undervaccinated countries.

“We’ve heard stories about wealthy counties giving doses to lower and middle income countries, and then … pointing fingers at receiving countries for not being able to use them [before they expire],” Veesler said. “That doesn’t really make sense.

“These are anecdotes, but they’re still stories that happen,” he added. “These superior storage properties might make a huge difference to reach people who still have not received vaccines.”

King’s lab designed the vaccine’s self-assembling protein nanoparticle technology — a vaccine-building strategy the lab developed in 2016. Veesler’s team integrated a key fragment of the coronavirus’ spike protein onto the nanoparticles.

SKYCovione, unlike Pfizer and Moderna vaccines, is made of proteins that form tiny particles studded with fragments of SARS-COV-2. That property makes the vaccine more stable and could enable broader vaccination efforts in parts of the world where medical and storage resources are harder to find, King said.

Protein-based vaccines are considered more traditional, King added, and have been used for decades to protect against hepatitis and other viral infections.

The researchers knew early on in the pandemic that while they were chipping away at building the technology behind the vaccine, manufacturing and distribution would be key.

So, through connections at the Gates Foundation, King and Veesler were introduced to South Korean biotech company SK bioscience, which has in-house vaccine manufacturing resources and has long developed immunizations abroad.

“In March and April 2020, we were already talking with SK and transferring our technology to them to really build that groundwork,” King said. “They did all the manufacturing and did all the clinical trials.”

The vaccine is South Korea’s first domestically manufactured COVID therapeutic, according to a statement from SK bioscience. The South Korean government has agreed to buy 10 million doses for domestic use.

In clinical trials, the vaccine was tested among more than 4,000 adults over the age of 18 and found to elicit about three times more antibodies than Covishield, the vaccine developed by AstraZeneca that does not have FDA approval, according to UW Medicine. The antibody conversion rate — the proportion of participants whose antibody levels increased fourfold or more — was also much higher with the UW-developed vaccine compared to Covishield.

No serious adverse reactions were recorded in any of the clinical trials.

While SKYCovione is arriving to the global public almost a year and a half after mRNA vaccines, its development has been “unbelievably fast” for protein-based vaccines, King said.

“Manufacturing speed is the key advantage of mRNA,” he said. “It just takes longer to manufacture proteins … But once you have it booted up, it scales beautifully.”

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87. Lin YR, Parks KR, Weidle C, Naidu AS, Khechaduri A, Riker AO, Takushi B, Chun JH, Borst AJ, Veesler D, Stuart A, Agrawal P, Gray M, Pancera M, Huang PS, Stamatatos L. HIV-1 VRC01 Germline-Targeting Immunogens Select Distinct Epitope-Specific B Cell Receptors. Immunity 2020 10; 53(4):840-851.e6. [PMID:33053332] [PMCID:PMC7735217]
88. McCallum M, Walls AC, Bowen JE, Corti D, Veesler D. Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation. Nat Struct Mol Biol 2020 10; 27(10):942-949. [PMID:32753755] [PMCID:PMC7541350]
89. Starr TN, Greaney AJ, Hilton SK, Ellis D, Crawford KHD, Dingens AS, Navarro MJ, Bowen JE, Tortorici MA, Walls AC, King NP, Veesler D, Bloom JD. Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding. Cell 2020 09; 182(5):1295-1310.e20. [PMID:32841599] [PMCID:PMC7418704]
90. Dingens AS, Crawford KHD, Adler A, Steele SL, Lacombe K, Eguia R, Amanat F, Walls AC, Wolf CR, Murphy M, Pettie D, Carter L, Qin X, King NP, Veesler D, Krammer F, Dickerson JA, Chu HY, Englund JA, Bloom JD. Serological identification of SARS-CoV-2 infections among children visiting a hospital during the initial Seattle outbreak. Nat Commun 2020 09; 11(1):4378. [PMID:32873791] [PMCID:PMC7463158]
91. Walls AC, Fiala B, Schäfer A, Wrenn S, Pham MN, Murphy M, Tse LV, Shehata L, O'Connor MA, Chen C, Navarro MJ, Miranda MC, Pettie D, Ravichandran R, Kraft JC, Ogohara C, Palser A, Chalk S, Lee EC, Kepl E, Chow CM, Sydeman C, Hodge EA, Brown B, Fuller JT, Dinnon KH, Gralinski LE, Leist SR, Gully KL, Lewis TB, Guttman M, Chu HY, Lee KK, Fuller DH, Baric RS, Kellam P, Carter L, Pepper M, Sheahan TP, Veesler D, King NP. Elicitation of potent neutralizing antibody responses by designed protein nanoparticle vaccines for SARS-CoV-2. bioRxiv 2020 Aug; [PMID:32817941] [PMCID:PMC7430571]
92. Erasmus JH, Khandhar AP, O'Connor MA, Walls AC, Hemann EA, Murapa P, Archer J, Leventhal S, Fuller JT, Lewis TB, Draves KE, Randall S, Guerriero KA, Duthie MS, Carter D, Reed SG, Hawman DW, Feldmann H, Gale M, Veesler D, Berglund P, Fuller DH. An Alphavirus-derived replicon RNA vaccine induces SARS-CoV-2 neutralizing antibody and T cell responses in mice and nonhuman primates. Sci Transl Med 2020 08; 12(555). [PMID:32690628] [PMCID:PMC7402629]
93. Ueda G, Antanasijevic A, Fallas JA, Sheffler W, Copps J, Ellis D, Hutchinson GB, Moyer A, Yasmeen A, Tsybovsky Y, Park YJ, Bick MJ, Sankaran B, Gillespie RA, Brouwer PJ, Zwart PH, Veesler D, Kanekiyo M, Graham BS, Sanders RW, Moore JP, Klasse PJ, Ward AB, King NP, Baker D. Tailored design of protein nanoparticle scaffolds for multivalent presentation of viral glycoprotein antigens. Elife 2020 08; 9. [PMID:32748788] [PMCID:PMC7402677]
94. Cao L, Goreshnik I, Coventry B, Case JB, Miller L, Kozodoy L, Chen RE, Carter L, Walls L, Park YJ, Stewart L, Diamond M, Veesler D, Baker D. De novo design of picomolar SARS-CoV-2 miniprotein inhibitors. bioRxiv 2020 Aug; [PMID:32793905] [PMCID:PMC7418719]
95. Pinto D, Park YJ, Beltramello M, Walls AC, Tortorici MA, Bianchi S, Jaconi S, Culap K, Zatta F, De Marco A, Peter A, Guarino B, Spreafico R, Cameroni E, Case JB, Chen RE, Havenar-Daughton C, Snell G, Telenti A, Virgin HW, Lanzavecchia A, Diamond MS, Fink K, Veesler D, Corti D. Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody. Nature 2020 07; 583(7815):290-295. [PMID:32422645]
96. Dingens AS, Crawford KHD, Adler A, Steele SL, Lacombe K, Eguia R, Amanat F, Walls AC, Wolf CR, Murphy M, Pettie D, Carter L, Qin X, King NP, Veesler D, Krammer F, Dickerson JA, Chu HY, Englund JA, Bloom JD. Serological identification of SARS-CoV-2 infections among children visiting a hospital during the initial Seattle outbreak. medRxiv 2020 Jun; [PMID:32511483] [PMCID:PMC7273251]
97. Starr TN, Greaney AJ, Hilton SK, Crawford KHD, Navarro MJ, Bowen JE, Tortorici MA, Walls AC, Veesler D, Bloom JD. Deep mutational scanning of SARS-CoV-2 receptor binding domain reveals constraints on folding and ACE2 binding. bioRxiv 2020 Jun; [PMID:32587970] [PMCID:PMC7310626]
98. McCallum M, Walls AC, Corti D, Veesler D. Closing coronavirus spike glycoproteins by structure-guided design. bioRxiv 2020 Jun; [PMID:32577661] [PMCID:PMC7302216]
99. Erasmus JH, Khandhar AP, Walls AC, Hemann EA, O'Connor MA, Murapa P, Archer J, Leventhal S, Fuller J, Lewis T, Draves KE, Randall S, Guerriero KA, Duthie MS, Carter D, Reed SG, Hawman DW, Feldmann H, Gale M, Veesler D, Berglund P, Fuller DH. Single-dose replicating RNA vaccine induces neutralizing antibodies against SARS-CoV-2 in nonhuman primates. bioRxiv 2020 May; [PMID:32511417] [PMCID:PMC7265689]
100. Mire CE, Chan YP, Borisevich V, Cross RW, Yan L, Agans KN, Dang HV, Veesler D, Fenton KA, Geisbert TW, Broder CC. A Cross-Reactive Humanized Monoclonal Antibody Targeting Fusion Glycoprotein Function Protects Ferrets Against Lethal Nipah Virus and Hendra Virus Infection. J Infect Dis 2020 05; 221(Suppl 4):S471-S479. [PMID:31686101] [PMCID:PMC7199785]
101. Crawford KHD, Eguia R, Dingens AS, Loes AN, Malone KD, Wolf CR, Chu HY, Tortorici MA, Veesler D, Murphy M, Pettie D, King NP, Balazs AB, Bloom JD. Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays. Viruses 2020 05; 12(5). [PMID:32384820] [PMCID:PMC7291041]
102. Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell 2020 04; 181(2):281-292.e6. [PMID:32155444] [PMCID:PMC7102599]
103. Pinto D, Park YJ, Beltramello M, Walls AC, Tortorici MA, Bianchi S, Jaconi S, Culap K, Zatta F, De Marco A, Peter A, Guarino B, Spreafico R, Cameroni E, Case JB, Chen RE, Havenar-Daughton C, Snell G, Telenti A, Virgin HW, Lanzavecchia A, Diamond MS, Fink K, Veesler D, Corti D. Structural and functional analysis of a potent sarbecovirus neutralizing antibody. bioRxiv 2020 Apr; [PMID:32511354] [PMCID:PMC7255795]
104. Parks KR, MacCamy AJ, Trichka J, Gray M, Weidle C, Borst AJ, Khechaduri A, Takushi B, Agrawal P, Guenaga J, Wyatt RT, Coler R, Seaman M, LaBranche C, Montefiori DC, Veesler D, Pancera M, McGuire A, Stamatatos L. Overcoming Steric Restrictions of VRC01 HIV-1 Neutralizing Antibodies through Immunization. Cell Rep 2019 12; 29(10):3060-3072.e7. [PMID:31801073] [PMCID:PMC6936959]
105. Park YJ, Walls AC, Wang Z, Sauer MM, Li W, Tortorici MA, Bosch BJ, DiMaio F, Veesler D. Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors. Nat Struct Mol Biol 2019 12; 26(12):1151-1157. [PMID:31792450] [PMCID:PMC7097669]
106. Dang HV, Chan YP, Park YJ, Snijder J, Da Silva SC, Vu B, Yan L, Feng YR, Rockx B, Geisbert TW [Dr. Thomas William Geisbert (born 1962)], Mire CE, Broder CC, Veesler D. An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections. Nat Struct Mol Biol 2019 10; 26(10):980-987. [PMID:31570878] [PMCID:PMC6858553]
107. Tortorici MA, Walls AC, Lang Y, Wang C, Li Z, Koerhuis D, Boons GJ, Bosch BJ, Rey FA, de Groot RJ, Veesler D. Structural basis for human coronavirus attachment to sialic acid receptors. Nat Struct Mol Biol 2019 06; 26(6):481-489. [PMID:31160783] [PMCID:PMC6554059]
108. Marcandalli J, Fiala B, Ols S, Perotti M, de van der Schueren W, Snijder J, Hodge E, Benhaim M, Ravichandran R, Carter L, Sheffler W, Brunner L, Lawrenz M, Dubois P, Lanzavecchia A, Sallusto F, Lee KK, Veesler D, Correnti CE, Stewart LJ, Baker D, Loré K, Perez L, King NP. Induction of Potent Neutralizing Antibody Responses by a Designed Protein Nanoparticle Vaccine for Respiratory Syncytial Virus. Cell 2019 03; 176(6):1420-1431.e17. [PMID:30849373] [PMCID:PMC6424820]
109. Walls AC, Xiong X, Park YJ, Tortorici MA, Snijder J, Quispe J, Cameroni E, Gopal R, Dai M, Lanzavecchia A, Zambon M, Rey FA, Corti D, Veesler D. Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion. Cell 2019 02; 176(5):1026-1039.e15. [PMID:30712865] [PMCID:PMC6751136]
110. Frenz B, Rämisch S, Borst AJ, Walls AC, Adolf-Bryfogle J, Schief WR, Veesler D, DiMaio F. Automatically Fixing Errors in Glycoprotein Structures with Rosetta. Structure 2019 01; 27(1):134-139.e3. [PMID:30344107] [PMCID:PMC6616339]
111. Tortorici MA, Veesler D. Structural insights into coronavirus entry. Adv Virus Res 2019; 105:93-116. [PMID:31522710] [PMCID:PMC7112261]
112. Park YJ, Lacourse KD, Cambillau C, DiMaio F, Mougous JD, Veesler D. Structure of the type VI secretion system TssK-TssF-TssG baseplate subcomplex revealed by cryo-electron microscopy. Nat Commun 2018 12; 9(1):5385. [PMID:30568167] [PMCID:PMC6300606]
113. Ting SY, Bosch DE, Mangiameli SM, Radey MC, Huang S, Park YJ, Kelly KA, Filip SK, Goo YA, Eng JK, Allaire M, Veesler D, Wiggins PA, Peterson SB, Mougous JD. Bifunctional Immunity Proteins Protect Bacteria against FtsZ-Targeting ADP-Ribosylating Toxins. Cell 2018 11; 175(5):1380-1392.e14. [PMID:30343895] [PMCID:PMC6239978]
114. Borst AJ, Weidle CE, Gray MD, Frenz B, Snijder J, Joyce MG, Georgiev IS, Stewart-Jones GB, Kwong PD, McGuire AT, DiMaio F, Stamatatos L, Pancera M, Veesler D. Germline VRC01 antibody recognition of a modified clade C HIV-1 envelope trimer and a glycosylated HIV-1 gp120 core. Elife 2018 11; 7. [PMID:30403372] [PMCID:PMC6237438]
115. Xu N, Veesler D, Doerschuk PC, Johnson JE. Allosteric effects in bacteriophage HK97 procapsids revealed directly from covariance analysis of cryo EM data. J Struct Biol 2018 05; 202(2):129-141. [PMID:29331608]
116. Snijder J, Ortego MS, Weidle C, Stuart AB, Gray MD, McElrath MJ, Pancera M, Veesler D, McGuire AT. An Antibody Targeting the Fusion Machinery Neutralizes Dual-Tropic Infection and Defines a Site of Vulnerability on Epstein-Barr Virus. Immunity 2018 04; 48(4):799-811.e9. [PMID:29669253] [PMCID:PMC5909843]
117. Xiong X, Tortorici MA, Snijder J, Yoshioka C, Walls AC, Li W, McGuire AT, Rey FA, Bosch BJ, Veesler D. Glycan Shield and Fusion Activation of a Deltacoronavirus Spike Glycoprotein Fine-Tuned for Enteric Infections. J Virol 2018 02; 92(4). [PMID:29093093] [PMCID:PMC5790929]
118. Borst AJ, James ZM, Zagotta WN, Ginsberg M, Rey FA, DiMaio F, Backovic M, Veesler D. The Therapeutic Antibody LM609 Selectively Inhibits Ligand Binding to Human αVβ3 Integrin via Steric Hindrance. Structure 2017 11; 25(11):1732-1739.e5. [PMID:29033288] [PMCID:PMC5689087]
119. Walls AC, Tortorici MA, Snijder J, Xiong X, Bosch BJ, Rey FA, Veesler D. Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion. Proc Natl Acad Sci U S A 2017 10; 114(42):11157-11162. [PMID:29073020] [PMCID:PMC5651768]
120. Nygren PJ, Mehta S, Schweppe DK, Langeberg LK, Whiting JL, Weisbrod CR, Bruce JE, Zhang J, Veesler D, Scott JD. Intrinsic disorder within AKAP79 fine-tunes anchored phosphatase activity toward substrates and drug sensitivity. Elife 2017 10; 6. [PMID:28967377] [PMCID:PMC5653234]
121. Frenz B, Walls AC, Egelman EH, Veesler D, DiMaio F. RosettaES: a sampling strategy enabling automated interpretation of difficult cryo-EM maps. Nat Methods 2017 Aug; 14(8):797-800. [PMID:28628127] [PMCID:PMC6009829]
122. Smith FD, Esseltine JL, Nygren PJ, Veesler D, Byrne DP, Vonderach M, Strashnov I, Eyers CE, Eyers PA, Langeberg LK, Scott JD. Local protein kinase A action proceeds through intact holoenzymes. Science 2017 06; 356(6344):1288-1293. [PMID:28642438] [PMCID:PMC5693252]
123. Yu X, Veesler D, Campbell MG, Barry ME, Asturias FJ, Barry MA, Reddy VS. Cryo-EM structure of human adenovirus D26 reveals the conservation of structural organization among human adenoviruses. Sci Adv 2017 May; 3(5):e1602670. [PMID:28508067] [PMCID:PMC5425241]
124. James ZM, Borst AJ, Haitin Y, Frenz B, DiMaio F, Zagotta WN, Veesler D. CryoEM structure of a prokaryotic cyclic nucleotide-gated ion channel. Proc Natl Acad Sci U S A 2017 04; 114(17):4430-4435. [PMID:28396445] [PMCID:PMC5410850]
125. Snijder J, Borst AJ, Dosey A, Walls AC, Burrell A, Reddy VS, Kollman JM, Veesler D. Vitrification after multiple rounds of sample application and blotting improves particle density on cryo-electron microscopy grids. J Struct Biol 2017 04; 198(1):38-42. [PMID:28254381] [PMCID:PMC5400742]
126. Walls A, Tortorici MA, Bosch BJ, Frenz B, Rottier PJ, DiMaio F, Rey FA, Veesler D. Crucial steps in the structure determination of a coronavirus spike glycoprotein using cryo-electron microscopy. Protein Sci 2017 01; 26(1):113-121. [PMID:27667334] [PMCID:PMC5192993]
127. Eshraghi A, Kim J, Walls AC, Ledvina HE, Miller CN, Ramsey KM, Whitney JC, Radey MC, Peterson SB, Ruhland BR, Tran BQ, Goo YA, Goodlett DR, Dove SL, Celli J, Veesler D, Mougous JD. Secreted Effectors Encoded within and outside of the Francisella Pathogenicity Island Promote Intramacrophage Growth. Cell Host Microbe 2016 Nov; 20(5):573-583. [PMID:27832588] [PMCID:PMC5384264]
128. Walls AC, Tortorici MA, Frenz B, Snijder J, Li W, Rey FA, DiMaio F, Bosch BJ, Veesler D. Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy. Nat Struct Mol Biol 2016 Oct; 23(10):899-905. [PMID:27617430] [PMCID:PMC5515730]
129. Yap ML, Klose T, Arisaka F, Speir JA, Veesler D, Fokine A, Rossmann MG. Role of bacteriophage T4 baseplate in regulating assembly and infection. Proc Natl Acad Sci U S A 2016 Mar; 113(10):2654-9. [PMID:26929357] [PMCID:PMC4791028]
130. Walls AC, Tortorici MA, Bosch BJ, Frenz B, Rottier PJM, DiMaio F, Rey FA, Veesler D. Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer. Nature 2016 Mar; 531(7592):114-117. [PMID:26855426] [PMCID:PMC5018210]
131. Gong Y, Veesler D, Doerschuk PC, Johnson JE. Effect of the viral protease on the dynamics of bacteriophage HK97 maturation intermediates characterized by variance analysis of cryo EM particle ensembles. J Struct Biol 2016 Mar; 193(3):188-195. [PMID:26724602]
132. Campbell MG, Veesler D, Cheng A, Potter CS, Carragher B. 2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy. Elife 2015 Mar; 4. [PMID:25760083] [PMCID:PMC4391500]
133. Krishnamurthy S, Veesler D, Khayat R, Snijder J, Huang R, Heck A, Johnson J, Anand GS. Distinguishing direct binding interactions from allosteric effects in the protease-HK97 prohead I δ domain complex by amide H/D exchange mass spectrometry. Bacteriophage ; 4(4):e959816. [PMID:26712354] [PMCID:PMC4588519]
134. Campbell MG, Kearney BM, Cheng A, Potter CS, Johnson JE, Carragher B, Veesler D. Near-atomic resolution reconstructions using a mid-range electron microscope operated at 200 kV. J Struct Biol 2014 Nov; 188(2):183-7. [PMID:25278130] [PMCID:PMC4497823]
135. Veesler D, Cupelli K, Burger M, Gräber P, Stehle T, Johnson JE. Single-particle EM reveals plasticity of interactions between the adenovirus penton base and integrin αVβ3. Proc Natl Acad Sci U S A 2014 Jun; 111(24):8815-9. [PMID:24889614] [PMCID:PMC4066496]
136. Veesler D, Khayat R, Krishnamurthy S, Snijder J, Huang RK, Heck AJ, Anand GS, Johnson JE. Architecture of a dsDNA viral capsid in complex with its maturation protease. Structure 2014 Feb; 22(2):230-7. [PMID:24361271] [PMCID:PMC3939775]
137. Spinelli S, Veesler D, Bebeacua C, Cambillau C. Structures and host-adhesion mechanisms of lactococcal siphophages. Front Microbiol 2014; 5:3. [PMID:24474948] [PMCID:PMC3893620]
138. Veesler D, Campbell MG, Cheng A, Fu CY, Murez Z, Johnson JE, Potter CS, Carragher B. Maximizing the potential of electron cryomicroscopy data collected using direct detectors. J Struct Biol 2013 Nov; 184(2):193-202. [PMID:24036281] [PMCID:PMC3832241]
139. Bebeacua C, Tremblay D, Farenc C, Chapot-Chartier MP, Sadovskaya I, van Heel M, Veesler D, Moineau S, Cambillau C. Structure, adsorption to host, and infection mechanism of virulent lactococcal phage p2. J Virol 2013 Nov; 87(22):12302-12. [PMID:24027307] [PMCID:PMC3807928]
140. Veesler D, Johnson JE. Cystovirus maturation at atomic resolution. Structure 2013 Aug; 21(8):1266-8. [PMID:23931138] [PMCID:PMC3779430]
141. Collins B, Bebeacua C, Mahony J, Blangy S, Douillard FP, Veesler D, Cambillau C, van Sinderen D. Structure and functional analysis of the host recognition device of lactococcal phage tuc2009. J Virol 2013 Aug; 87(15):8429-40. [PMID:23698314] [PMCID:PMC3719809]
142. Desmyter A, Farenc C, Mahony J, Spinelli S, Bebeacua C, Blangy S, Veesler D, van Sinderen D, Cambillau C. Viral infection modulation and neutralization by camelid nanobodies. Proc Natl Acad Sci U S A 2013 Apr; 110(15):E1371-9. [PMID:23530214] [PMCID:PMC3625315]
143. Veesler D, Ng TS, Sendamarai AK, Eilers BJ, Lawrence CM, Lok SM, Young MJ, Johnson JE, Fu CY. Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography. Proc Natl Acad Sci U S A 2013 Apr; 110(14):5504-9. [PMID:23520050] [PMCID:PMC3619359]
144. Snijder J, Rose RJ, Veesler D, Johnson JE, Heck AJ. Studying 18 MDa virus assemblies with native mass spectrometry. Angew Chem Int Ed Engl 2013 Apr; 52(14):4020-3. [PMID:23450509] [PMCID:PMC3949431]
145. Bebeacua C, Lai L, Vegge CS, Brøndsted L, van Heel M, Veesler D, Cambillau C. Visualizing a complete Siphoviridae member by single-particle electron microscopy: the structure of lactococcal phage TP901-1. J Virol 2013 Jan; 87(2):1061-8. [PMID:23135714] [PMCID:PMC3554098]
146. Campbell MG, Cheng A, Brilot AF, Moeller A, Lyumkis D, Veesler D, Pan J, Harrison SC, Potter CS, Carragher B, Grigorieff N. Movies of ice-embedded particles enhance resolution in electron cryo-microscopy. Structure 2012 Nov; 20(11):1823-8. [PMID:23022349] [PMCID:PMC3510009]
147. Veesler D, Quispe J, Grigorieff N, Potter CS, Carragher B, Johnson JE. Maturation in action: CryoEM study of a viral capsid caught during expansion. Structure 2012 Aug; 20(8):1384-90. [PMID:22748764] [PMCID:PMC3418467]
148. Veesler D, Spinelli S, Mahony J, Lichière J, Blangy S, Bricogne G, Legrand P, Ortiz-Lombardia M, Campanacci V, van Sinderen D, Cambillau C. Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism. Proc Natl Acad Sci U S A 2012 Jun; 109(23):8954-8. [PMID:22611190] [PMCID:PMC3384155]
149. Veesler D, Johnson JE. Virus maturation. Annu Rev Biophys 2012; 41:473-96. [PMID:22404678] [PMCID:PMC3607295]
150. Veesler D, Cambillau C. A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries. Microbiol Mol Biol Rev 2011 Sep; 75(3):423-33, first page of table of contents. [PMID:21885679] [PMCID:PMC3165541]
151. Shepherd DA, Veesler D, Lichière J, Ashcroft AE, Cambillau C. Unraveling lactococcal phage baseplate assembly by mass spectrometry. Mol Cell Proteomics 2011 Sep; 10(9):M111.009787. [PMID:21646642] [PMCID:PMC3186816]
152. Goulet A, Lai-Kee-Him J, Veesler D, Auzat I, Robin G, Shepherd DA, Ashcroft AE, Richard E, Lichière J, Tavares P, Cambillau C, Bron P. The opening of the SPP1 bacteriophage tail, a prevalent mechanism in Gram-positive-infecting siphophages. J Biol Chem 2011 Jul; 286(28):25397-405. [PMID:21622577] [PMCID:PMC3137110]
153. Bebeacua C, Bron P, Lai L, Vegge CS, Brøndsted L, Spinelli S, Campanacci V, Veesler D, van Heel M, Cambillau C. Structure and molecular assignment of lactococcal phage TP901-1 baseplate. J Biol Chem 2010 Dec; 285(50):39079-86. [PMID:20937834] [PMCID:PMC2998104]
154. Veesler D, Robin G, Lichière J, Auzat I, Tavares P, Bron P, Campanacci V, Cambillau C. Crystal structure of bacteriophage SPP1 distal tail protein (gp19.1): a baseplate hub paradigm in gram-positive infecting phages. J Biol Chem 2010 Nov; 285(47):36666-73. [PMID:20843802] [PMCID:PMC2978595]
155. Campanacci V, Veesler D, Lichière J, Blangy S, Sciara G, Moineau S, van Sinderen D, Bron P, Cambillau C. Solution and electron microscopy characterization of lactococcal phage baseplates expressed in Escherichia coli. J Struct Biol 2010 Oct; 172(1):75-84. [PMID:20153432]
156. Veesler D, Blangy S, Lichière J, Ortiz-Lombardía M, Tavares P, Campanacci V, Cambillau C. Crystal structure of Bacillus subtilis SPP1 phage gp23.1, a putative chaperone. Protein Sci 2010 Sep; 19(9):1812-6. [PMID:20665904] [PMCID:PMC2975145]
157. Veesler D, Blangy S, Spinelli S, Tavares P, Campanacci V, Cambillau C. Crystal structure of Bacillus subtilis SPP1 phage gp22 shares fold similarity with a domain of lactococcal phage p2 RBP. Protein Sci 2010 Jul; 19(7):1439-43. [PMID:20506290] [PMCID:PMC2974835]
158. Veesler D, Dreier B, Blangy S, Lichière J, Tremblay D, Moineau S, Spinelli S, Tegoni M, Plückthun A, Campanacci V, Cambillau C. Crystal structure and function of a DARPin neutralizing inhibitor of lactococcal phage TP901-1: comparison of DARPin and camelid VHH binding mode. J Biol Chem 2009 Oct; 284(44):30718-26. [PMID:19740746] [PMCID:PMC2781625]
159. Veesler D, Blangy S, Siponen M, Vincentelli R, Cambillau C, Sciara G. Production and biophysical characterization of the CorA transporter from Methanosarcina mazei. Anal Biochem 2009 May; 388(1):115-21. [PMID:19233118]
160. Veesler D, Blangy S, Cambillau C, Sciara G. There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization. Acta Crystallogr Sect F Struct Biol Cryst Commun 2008 Oct; 64(Pt 10):880-5. [PMID:18931428] [PMCID:PMC2564894]