Anti-SV40 VP2 + VP3抗体

靶点信息

Isoform VP2. Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly. The viral progenies exit the cells by lytic release. Isoform VP2 may repress SP1 activation of the SV40 early promoter, via specific protein-protein and protein-DNA interactions.. Isoform VP3. Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus entry, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane. Essential for focus formation and virus endoplasmic reticulum-to-cytosol membrane transport, required to recruit selective cellular components to the foci in the ER membrane. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Isoform VP3 represses SP1 activation of the SV40 early promoter, via specific protein-protein and protein-DNA interactions. SP1 additionally participates in recruiting VP3 to the SV40 minichromosome during SV40 assembly. Plays a role in virion assembly within the nucleus. May initiate host cell lysis when associated with VP4.. Isoform VP4. Viroporin inducing perforation of cellular membranes to trigger virus progeny release. Forms pores of 3 nm inner diameter. VP4 is expressed about 24 hours after the late structural proteins and is not incorporated into the mature virion.