BK polyomavirus minor capsid protein VP2 (VP2)

The BK polyomavirus minor capsid protein VP2 is a structural component of the BKPyV virion, situated beneath the outer VP1 shell. It plays a critical role in the viral life cycle, particularly during the entry phase where it facilitates the escape of the viral genome from the endoplasmic reticulum into the cytosol and subsequently the nucleus [1][6]. VP2 contains a highly hydrophobic N-terminal sequence that acts as a viroporin-like element, essential for membrane penetration during infection [1]. In clinical contexts, BK polyomavirus is a significant pathogen for transplant recipients, leading to BK polyomavirus-associated nephropathy (BKVAN) in kidney transplants and hemorrhagic cystitis in hematopoietic stem cell transplant patients [7][8]. While there are currently no FDA-approved drugs that specifically and exclusively target VP2, it is a focal point for the development of novel entry inhibitors and multi-valent virus-like particle (VLP) vaccines [10][14]. Experimental peptides derived from VP2, such as D1min, have demonstrated potent antiviral activity by blocking the interaction between VP2 and the VP1 pore, thereby preventing viral uncoating [2][3].

Other names

Minor capsid protein VP2BKPyV VP2BKV VP2VP2 protein

Inhibition of viral entry and uncoating by blocking VP2-VP1 interaction