Simian Virus type 40 Major Capsid VP1 (DAG-P2866)

Simian Virus type 40 Major Capsid VP1 (full length), recombinant protein from S. cerevisiae

Product Overview
Simian Virus 40 (SV40) Simian Virus 40 Major Capsid VP1 full length protein
Nature
Recombinant
Tag/Conjugate
Unconjugated
Cellular Localization
Virion. Nucleus. Endoplasmic reticulum. Note=Following host cell entry, the virion enters into the endoplasmic reticulum through a calveolar-dependent pathway. Then, viral DNA is translocated to the nucleus. Shortly after synthesis, a nuclear localization
Procedure
None
Format
Lyophilised
Buffer
Preservative: None Constituents: PBS
Preservative
None
Storage
Store at +4°C. Preservative: None Constituents: PBS
Reconstitution
Reconstitute with deionized H2O.
Introduction
Simian virus 40 (SV40) is a small, non enveloped DNA virus with an icosahedral capsid of 45 nm.
Antigen Description
The simian virus 40 capsid is composed of 72 pentamers of VP1, the major protein of SV40. These pentamers are arranged in a T=7d icosahedral surface lattice, which is maintained by three types of appropriately arranged, non-equivalent interactions between the pentamers. Simian Virus 40 Major Capsid VP1 binds to N-glycolylneuraminic analog of the ganglioside GM1 on the cell surface to provide virion attachment to target cell. Once attached, the virion enters a caveolae and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. The assembly takes place in the cell nucleus, encapsulates the genomic DNA and participates in rearranging nucleosomes around the viral DNA. The viral progenies exit the cells by lytic release.
Keywords
SV40 Major Capsid VP1; Major capsid protein VP1; Major structural protein VP1

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References


THE USE OF ADDITIVE AND SUBTRACTIVE APPROACHES TO EXAMINE THE NUCLEAR-LOCALIZATION SEQUENCE OF THE POLYOMAVIRUS MAJOR CAPSID PROTEIN-VP1

VIROLOGY

Authors: CHANG, DC; HAYNES, JI; BRADY, JN; CONSIGLI, RA

The Merkel Cell Polyomavirus Minor Capsid Protein

PLOS PATHOGENS

Authors: Schowalter, Rachel M.; Buck, Christopher B.

The surface of polyomavirus virions is composed of pentameric knobs of the major capsid protein, VP1. In previously studied polyomavirus species, such as SV40, two interior capsid proteins, VP2 and VP3, emerge from the virion to play important roles during the infectious entry process. Translation of the VP3 protein initiates at a highly conserved Met-Ala-Leu motif within the VP2 open reading frame. Phylogenetic analyses indicate that Merkel cell polyomavirus ( MCV or MCPyV) is a member of a divergent clade of polyomaviruses that lack the conserved VP3 N-terminal motif. Consistent with this observation, we show that VP3 is not detectable in MCV-infected cells, VP3 is not found in native MCV virions, and mutation of possible alternative VP3-initiating methionine codons did not significantly affect MCV infectivity in culture. In contrast, VP2 knockout resulted in a > 100-fold decrease in native MCV infectivity, despite normal virion assembly, viral DNA packaging, and cell attachment. Although pseudovirus-based experiments confirmed that VP2 plays an essential role for infection of some cell lines, other cell lines were readily transduced by pseudovirions lacking VP2. In cell lines where VP2 was needed for efficient infectious entry, the presence of a conserved myristoyl modification on the N-terminus of VP2 was important for its function. The results show that a single minor capsid protein, VP2, facilitates a post-attachment stage of MCV infectious entry into some, but not all, cell types.

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