BK polyomavirus minor capsid protein VP2 (VP2) (VP2)

BK polyomavirus capsid protein VP2 (also known as minor capsid protein VP2) is a structural component of the BK polyomavirus (BKPyV), a double-stranded DNA virus that establishes lifelong latent infections in the human urinary tract (UniProt P03094). VP2 is located internally within the icosahedral capsid shell formed by the major protein VP1 and is essential for the viral life cycle, participating in host cell receptor binding, endosomal escape, and nuclear entry (PubMed 31961322). The protein contains a conserved C-terminal DNA-binding domain and a nuclear localization signal that are critical for the encapsidation of the viral genome and its subsequent delivery to the host nucleus (UniProt P03094). During the infection process, VP2 and the related VP3 protein are exposed in the endoplasmic reticulum, where they may function as viroporins to facilitate the translocation of the viral genome into the cytosol (PubMed 21613584). In immunocompromised patients, particularly kidney transplant recipients, BKPyV reactivation leads to BK polyomavirus-associated nephropathy (BKVAN), which can result in graft loss (PubMed 29115154). While no specific antivirals targeting VP2 are currently approved, it remains a significant target for research; for instance, experimental peptides derived from the VP2 sequence have been shown to inhibit infection by blocking the VP1-VP2/3 binding interface (PubMed 31961322).

Other names

BK polyomavirus capsid protein VP2Minor structural protein VP2VP2_POVBKMinor capsid protein VP2

There are currently no approved drugs that directly target the BK polyomavirus VP2 protein. Experimental strategies focus on disrupting the interaction between VP2/3 and the major capsid protein VP1 using peptides or targeting host factors like CFTR that are required for VP2 exposure during infection (PubMed 31961322, PubMed 31535055).