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Domain

The N-terminus of VP1 is sequestered within the mature capsid. It contains a phospholipase A2-like region and putative nuclear localization signals.

Function

Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of three size variants of the capsid protein VP1, VP2 and VP3 which differ in their N-terminus. The capsid encapsulates the genomic ssDNA. Binds to host cell heparan sulfate and uses host ITGA5-ITGB1 as coreceptor on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptor also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus.

Sequence similarities

Belongs to the parvoviridae capsid protein family.

Cellular localization

  • Virion
  • Host nucleus
  • Host nucleolus
  • Capsid proteins are first observed in the host nucleolus where capsid assembly may occur, and then are present over the whole nucleoplasm where encapsidation of the viral DNA takes place.

Alternative names

Capsid protein VP1, VP1

Target type

Proteins

Primary research area

Neuroscience

Molecular weight

81945Da

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