BK polyomavirus major capsid protein VP1 (VP1)

BK polyomavirus major capsid protein VP1 is the principal structural protein of the BK polyomavirus, self-assembling into pentamers that form the external shell of the icosahedral viral capsid with T=7 symmetry and a diameter of approximately 50 nm[2][4][7]. The capsid comprises 72 pentameric units of VP1 stabilized by intermolecular disulfide bonds, in association with minor structural proteins VP2 and VP3, and it encapsulates the viral DNA genome[2][7]. VP1 is responsible for virion attachment to host cells by binding specific sialic acid–containing ganglioside receptors (notably GT1b and GD1b) on the cell surface, facilitating viral entry predominantly via caveolin-mediated endocytosis[3][4]. In addition to its structural role, VP1 interacts with host cell factors and participates in the uncoating process inside the host cell, which is required for delivery of the viral genome to the nucleus for replication[4]. Due to its critical roles in the infectious process and immune recognition, VP1 is a key target for antiviral strategies, diagnostic assays, and vaccine development for BK polyomavirus–related diseases[5].

Other names

Major capsid protein VP1Major structural protein VP1BKPyV VP1Polyomavirus coat protein VP1

Experimental peptides inhibit viral infection by binding to the central pore of VP1 pentamers, blocking critical interactions required for viral infectivity[1].