Major capsid protein VP1 (BK polyomavirus) (BKV VP1)

The Major capsid protein VP1 is the primary structural component of the BK polyomavirus (BKV), a double-stranded DNA virus that is highly prevalent in the human population. Structurally, 360 copies of VP1 organize into 72 pentamers to form a T=7 icosahedral capsid, which protects the viral genome and serves as the primary interface with the host cell [4, 12, 22]. VP1 is essential for the viral lifecycle, as it mediates attachment to host cell ganglioside receptors (specifically GT1b and GD1b) and facilitates viral entry through caveolin-mediated endocytosis [4, 11, 15]. While BKV remains latent in the urinary tract of most individuals, it can reactivate under conditions of immunosuppression, leading to BK virus-associated nephropathy (BKVAN) in kidney transplant recipients and hemorrhagic cystitis in hematopoietic stem cell transplant patients [12, 18, 21]. Because VP1 is the only protein exposed on the surface of the virion, it is a key target for neutralizing antibodies and vaccine development [3, 9]. Therapeutic strategies currently focus on monoclonal antibodies, such as MAU868 (traxivitug), which bind with high affinity to conserved residues in the VP1 loops to block viral binding and entry [1, 5, 7]. These targeted therapies aim to reduce viral load and prevent the progression of BKV-associated diseases without the need to decrease essential immunosuppressive regimens, which often carry the risk of organ rejection [3, 13, 18].

Other names

Major structural protein VP1Capsid protein VP1BKPyV VP1VP1

Neutralization of viral particles, inhibition of host cell ganglioside receptor binding, and blocking of viral entry and uncoating processes.