JC virus major capsid protein VP1 (VP1)

The JC virus major capsid protein VP1 is the primary structural component of the JC polyomavirus (JCPyV) capsid, organized into 72 pentamers that form an icosahedral shell (UniProt P03089). It plays a critical role in the viral life cycle by mediating attachment to host cells through specific interactions with alpha-2,6-linked sialic acid on the lactoseries tetrasaccharide c (LSTc) glycan (PubMed: 20308598). Beyond entry, VP1 is essential for the assembly of new virions and the packaging of the viral genome. In the context of disease, JCPyV is the causative agent of progressive multifocal leukoencephalopathy (PML), a severe demyelinating disease of the central nervous system that typically emerges in severely immunocompromised patients or those on specific immunomodulatory therapies (NIH: NINDS PML Information). Mutations in the surface loops of VP1 are frequently observed in PML patients, which may alter receptor specificity and facilitate neuroinvasion (PubMed: 23698303). Therapeutic efforts targeting VP1 include the development of neutralizing antibodies and small molecules designed to block viral entry or disrupt capsid formation, although no specific antiviral therapy is currently FDA-approved for this target.

Other names

Major capsid protein VP1JCPyV VP1Polyomavirus JC VP1Capsid protein 1

Inhibition of viral attachment to host cell receptors and interference with viral capsid assembly