Disease relevance of HpVgp6

• These results suggest that JC virus VP1 can be transported into the nucleus and self-assembled to form capsid-like particles without the involvement of the viral minor capsid proteins, VP2 and VP3 [1].
• Although the major capsid protein VP1 is involved in endocytosis, and largely defines virion structure, the functions of the minor proteins VP2 and VP3 have remained obscure [2].
• A complex of the polyomavirus internal protein VP2/VP3 with the pentameric major capsid protein VP1 has been prepared by co-expression in Escherichia coli [3].
• Nucleotides sequence of the genes for the simian virus 40 proteins VP2 and VP3 [4].
• The tryptic peptides of VP1, VP3, VP4, and VP5 combined of SV40 were compared with those of the same polypeptides of BK virus [5].

High impact information on HpVgp6

• Using two-dimensional polyacrylamide gel electrophoresis and well characterized deletion mutants of SV40 that produce proteins of smaller size, we show that these two proteins are, indeed, the virus-coded proteins VP1 and VP3 [6].
• The codons of the COOH-terminal amino acids of VP2 and VP3 are read in a second phase as the codons of the NH2-terminal amino acids of VP1 [4].
• The sequence information needed for assigning genotypes can be captured by VP1, VP2, VP3, or large T-gene sequencing [7].
• We tested whether an internal ribosome entry site (IRES) might be located upstream of the VP3 AUG that would facilitate its utilization, especially late in infection when cap-dependent translation is reduced (19) [8].
• VP2 and VP3, but not VP1, caused the permeabilization of bacterial membranes [9].

Chemical compound and disease context of HpVgp6

• Tryptic peptide analysis demonstrated that the 74K protein shares methionine- and serine-containing peptides with VP1 and VP3 and thus is structurally related to the capsid proteins [10].

Biological context of HpVgp6

• From the DNA sequence the sizes and sequences of VP2 and VP3 could be predicted [11].
• This region contains the coding sequence for VP3 and a portion of VP2, but does not include the late promoters or the coding sequence for the late leaders [12].
• Insertion of this strong initiation signal at the same site, but in a different reading frame, resulted in the synthesis of VP3 at one-third of the wild-type rate [13].
• The intranuclear location of simian virus 40 polypeptides VP2 and VP3 depends on a specific amino acid sequence [14].
• Newer evidence suggests that this model is incorrect, and that protein VP1 is a product of one viral gene and that the multiple components of VP2 and VP3 are products of a second viral gene [15].

Anatomical context of HpVgp6

• It is concluded that at least part of the sequence of VP2 amino acids 317 to 323 allows VP2 and VP3 to remain stably located inside the cell nucleus [14].
• In this work, the translation initiation mechanism of VP3 was investigated in chicken embryo fibroblast cells by transfection of a series of BFDV mutant clones and transient reporter gene chloramphenicol acetyltransferase (CAT) expression assay, leading to the conclusion that BFDV VP3 was translated by leaky ribosomal scanning [16].
• The antibodies recognize VP2 and VP3 in infected cells by immunofluorescence and in subcellular fractions by ELISA [17].

Associations of HpVgp6 with chemical compounds

• Treatment of the virion-derived 110S nucleoprotein complex with 0.25% Sarkosyl dissociated VP2, VP3, and histones, leaving a stable VP1-DNA complex [18].
• As shown by construction of hybrid virus genomes and site-directed mutagenesis, a single amino acid difference (glycine instead of valine or alanine) within the common region of the minor structural proteins VP2/VP3 is responsible for this type of abortive infection of CE cells [19].

Analytical, diagnostic and therapeutic context of HpVgp6

• As for PCR, VP3 was amplified in all 14 cases and TCR in 9 cases [20].
• VP-2 and VP-3 are related by tryptic peptide mapping to each other but not to VP-1 [21].

References