Summary of mAbs,Abs,bNAbs that attach to E1 E2

Click on the pointers to learn about the different antibodies and mAbs that attach at various regions of the E1 E2 protein. The graphic can be expanded to a full window for a better view. This is a general overview of the summarized data.

Feeling curious? Scroll down below to learn more about specific regions of E1 E2 and some fun facts about some of the mAbs or Abs that attach to those epitopes.

Amino Acids 192-211

Antibodies -H-111

The H-111 antibody, derived from an HCV-infected donor (Keck et. al. 2004b), targets a conserved epitope on the E1 protein, exhibiting cross-genotype reactivity and blocking virus entry. Analysis reveals somatic mutations indicating affinity maturation. H-111 neutralizes HCV-like particles and infectious virions, suggesting therapeutic potential.

Amino Acids 312-327

Antibodies - IGH505, IGH526

Human monoclonal antibodies (MAbs) IGH505 and IGH526, sourced from an individual who cleared HCV post-therapy, display robust neutralization against diverse HCV-pseudotyped particles (HCVpp), spanning genotypes 1a, 1b, 4a, 5a, and 6a (for the mapping purposes in the visualization, we used wild type protein sequence so there might be a few differences), albeit with reduced efficacy against genotype 2a. Their epitopes, mapped on the HCV E1 glycoprotein, underscore their specificity.

Amino Acids 412-423

Antibodies - HCV-1, 95-2, FAb e137, MBL-HCV1, AP33 (MRCT10.v362), HC33, mu5B3 (hu5B3.v3) (humanized)

AP33- One of the most studied monoclonal antibodies AP33 in the context of HCV infection neutralization. AP33 targeted a conserved linear epitope, holding promise for broad-spectrum vaccine and therapeutic antibody development. AP33 is what we call a bNAb; broadly neutralizing antibody.

Amino Acids 418-446

Antibodies - HC84.1, HC-84.20, HC-84.21, HC-84.22, HC-84.23, HC-84.24, HC-84.25, HC-84.26, HC-84.27

These epitopes mediate broad virus neutralization, essential for vaccine design. Hence they are very promising to act as targets for a vaccine.

Amino Acids 523 to 535

Antibodies - Fab e20, CBH5, HC-1, HC-11, AR3D, AR3C, AR3B, AR3A, CBH-5, e137

AR3A, AR3B, AR3C, and AR3D are broadly neutralizing antibodies, hence they are promising in the context of future vaccine development.

Amino Acids 639 to 660

Antibodies - AR5A, HC84-27

HC84-27 and other mAbs in this series as reported in the linked study attached to various regions during the assays in a study reported by Keck et.al. in 2012. This is exciting as it gives room for making a vaccine that could be targetted to various regions.

Amino Acid 698

Antibodies - AR4A

AR4A targets a specific epitope on the E1E2 glycoprotein complex of HCV. This epitope is distinct from the CD81 binding site (CD81bs) on E2, suggesting that AR4A binds to a different region of the glycoprotein complex.he binding of AR4A to its epitope requires proper folding of the E1E2 glycoprotein complex. Mutations that disrupt the quaternary structure of E1E2 also abolish the binding of AR4A, indicating that the epitope recognized by AR4A is dependent on the correct conformation of the glycoprotein complex.

Unspecified E2 Regions

Antibodies - L1, L3, CBH4B, CBH4D, CBH4G, U1, HMabs 212, AB6865, AB68

These are the mAbs and Abs that we know attach to E1 and E2 however specific regions are yet to be identified.

A lot of these HCV antibodies target conserved epitopes on E2, inhibiting its binding to CD81. They act outside the CD81-binding site, possibly by preventing E2 conformational changes necessary for CD81 interaction.

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