Enterovirus 71 capsid protein VP1 (VP1)

Enterovirus 71 capsid protein VP1 is a major structural protein (297 amino acids, 32 kDa) forming the outer surface of the icosahedral viral capsid, alongside VP2, VP3, and internal VP4. It constitutes the "canyon" depression around five-fold axes and contains a hydrophobic pocket binding a stabilizing "pocket factor" (likely a lipid).[1][2] VP1 mediates receptor binding to host receptors like PSGL-1 and SCARB2 via surface loops (e.g., BC, GH, HI), initiating uncoating: receptor engagement expels the pocket factor, destabilizes the capsid, forms an expanded A-particle expelling VP4, exposes VP1 N-terminus (residues 1-71 interacting with viral RNA), and opens channels for genome release into the cytosol.[1][2][3] Key residues like VP1-145 (Q/G/E switch for receptor tropism and virulence) and VP1-244 modulate binding and pathogenesis.[1][4][7] Surface loops are variable, hosting neutralizing epitopes targeted by monoclonal antibodies (e.g., mAb 2G8, mAb51) and VP1-based recombinant vaccines.[1] VP1 gene sequences define EV71 genogroups (A, B1-B5, C1-C5) for identification.[1] Small-molecule inhibitors like WIN 51711 bind the VP1 pocket without conformational change, stabilizing the virion against uncoating.[2] As a viral protein essential for assembly, entry, and infection, VP1 is a key therapeutic target for antivirals and vaccines against EV71-associated hand-foot-mouth disease and neurological complications.[1][2]

Other names

EV71 VP1Enterovirus A71 VP1 protein

Stabilizes virion by binding VP1 hydrophobic pocket, Prevents pocket factor displacement, Restricts capsid dynamics for genome release, Inhibits uncoating