Viruses, being obligate intracellular parasites, are completely dependent on their host for replication and multiplication. This involves gaining entry into susceptible cells and diverting cellular resources like protein synthesis machinery towards producing multiple copies of viral proteins. Hence, viruses have co-evolved with their hosts to develop several strategies to mimic host proteins, either at the structural level or at the sequence level. This allows the virus to efficiently overtake key cellular processes, which shifts the equilibrium toward the synthesis of viral proteins. The coronavirus spike hijacks the host's shuttling protein, referred to as COPI, from Golgi to arrive at the site of virus assembly (i.e., ERGIC). A short C-terminal di-basic motif (K-x-H-x-x) of spike that resembles host di-basic motifs (K-x-K/H-x-x) mediates this interaction. My current research is geared towards understanding how the different upstream and downstream residues contribute to this molecular hijacking.

Viroporins are small membrane proteins of viral origin that facilitate various steps of the viral lifecycle. These proteins are expressed by a diverse set of viruses and have been reported to target nearly every host cell membrane and compartment, including endocytic and exocytic vesicles, the ER, mitochondria, the Golgi, and the plasma membrane. Viroporins, like the alphavirus 6K, influenza virus M2, HIV Vpu, HCV p7, SARS-2 E, SARS-2 orf3a, HAV 2B, and VP4, typically form ion channels or small discrete pores as homo-oligomers. My research interest in viroporins started during my PhD, and since then, I have worked on the alphavirus 6K, HAV-VP4, HAV-2B, and the FHV gamma peptide, respectively. My research on chikungunya virus 6K established it as a key therapeutic target against chikungunya and possibly other alphaviruses.