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The BK virus major capsid protein VP1 is the primary structural component of the BK polyomavirus (BKV) virion, forming the icosahedral shell that encapsulates the viral DNA [UniProt: P03088]. It plays a fundamental role in the viral infection cycle by mediating attachment to host cells through interactions with sialic acid-containing gangliosides, specifically GD1b and GT1b [PubMed: 29439211]. Following attachment, VP1 facilitates viral entry into the host cell via endocytosis, making it essential for the initiation of infection. Upon reactivation in immunocompromised patients, such as renal transplant recipients, BKV causes significant morbidity, including BK virus-associated nephropathy (BKVAN) and hemorrhagic cystitis [PubMed: 31437156]. Because VP1 is the most exposed protein on the viral surface, it serves as the dominant target for neutralizing antibodies produced by the host immune system. Therapeutic strategies targeting VP1 include the development of monoclonal antibodies, such as MAU868, which aim to block viral entry and prevent the spread of the virus [NCT04294472]. Additionally, VP1 is a key candidate for virus-like particle (VLP) vaccines designed to elicit protective immunity in high-risk populations.
Neutralization of viral particles by blocking attachment to host cell receptors and preventing viral entry.
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