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Gene Review

HpVgp6  -  capsid protein

Hamster polyomavirus

 
 
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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

  1. Self-assembly of the JC virus major capsid protein, VP1, expressed in insect cells. Chang, D., Fung, C.Y., Ou, W.C., Chao, P.C., Li, S.Y., Wang, M., Huang, Y.L., Tzeng, T.Y., Tsai, R.T. J. Gen. Virol. (1997) [Pubmed]
  2. Myristic acid is coupled to a structural protein of polyoma virus and SV40. Streuli, C.H., Griffin, B.E. Nature (1987) [Pubmed]
  3. Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry. Chen, X.S., Stehle, T., Harrison, S.C. EMBO J. (1998) [Pubmed]
  4. Nucleotides sequence of the genes for the simian virus 40 proteins VP2 and VP3. Reddy, V.B., Dhar, R., Weissman, S.M. J. Biol. Chem. (1978) [Pubmed]
  5. Virion polypeptide composition of the human papovavirus BK: comparison with simian virus 40 and polyoma virus. Wright, P.J., Di Mayorca, G. J. Virol. (1975) [Pubmed]
  6. Coupled transcription-translation of DNA injected into Xenopus oocytes. De Robertis, E.M., Mertz, J.E. Cell (1977) [Pubmed]
  7. Phylogenetic analysis of polyomavirus BK sequences. Sharma, P.M., Gupta, G., Vats, A., Shapiro, R., Randhawa, P. J. Virol. (2006) [Pubmed]
  8. 19S late mRNAs of simian virus 40 have an internal ribosome entry site upstream of the virion structural protein 3 coding sequence. Yu, Y., Alwine, J.C. J. Virol. (2006) [Pubmed]
  9. Simian virus 40 late proteins possess lytic properties that render them capable of permeabilizing cellular membranes. Daniels, R., Rusan, N.M., Wilbuer, A.K., Norkin, L.C., Wadsworth, P., Hebert, D.N. J. Virol. (2006) [Pubmed]
  10. A simian virus 40-encoded protein of Mr 74,000 daltons is structurally related to the capsid proteins of the virus. Krippl, B., Dreiseikelmann, B., Werchau, H. J. Cell. Biochem. (1983) [Pubmed]
  11. Polyoma virus DNA: Sequence from the late region that specifies the leader sequence for late mRNA and codes for VP2, VP3, and the N-terminus of VP1. Arrand, J.R., Soeda, E., Walsh, J.E., Smolar, N., Griffin, B.E. J. Virol. (1980) [Pubmed]
  12. Mutation affecting late gene expression in polyoma virus maps in the late region. Thomas, E.K., Hare, J.D. J. Virol. (1982) [Pubmed]
  13. Mechanisms of synthesis of virion proteins from the functionally bigenic late mRNAs of simian virus 40. Sedman, S.A., Mertz, J.E. J. Virol. (1988) [Pubmed]
  14. The intranuclear location of simian virus 40 polypeptides VP2 and VP3 depends on a specific amino acid sequence. Wychowski, C., Benichou, D., Girard, M. J. Virol. (1987) [Pubmed]
  15. Structural proteins of polyoma virus: proteolytic degradation of virion proteins by exogenous and by virion-associated proteases. Friedmann, T. J. Virol. (1976) [Pubmed]
  16. Evidence for translation of VP3 of avian polyomavirus BFDV by leaky ribosomal scanning. Liu, Q., Hobom, G. Arch. Virol. (2000) [Pubmed]
  17. Antipeptide antibodies directed against the carboxy-terminal region of SV40 structural proteins VP2 and VP3. Streckert, H.J., Brüssow, H., Sure, K., Werchau, H. J. Cell. Biochem. (1986) [Pubmed]
  18. Stable association of viral protein VP1 with simian virus 40 DNA. Brady, J.N., Lavialle, C.A., Radonovich, M.F., Salzman, N.P. J. Virol. (1981) [Pubmed]
  19. Host restriction in the productive cycle of avian polyomavirus budgerigar fledgling disease virus type 3 depends on a single amino acid change in the common region of structural proteins VP2/VP3. Stoll, R., Hobom, G., Müller, H. J. Gen. Virol. (1994) [Pubmed]
  20. JC virus early protein detection by immunohistochemistry in progressive multifocal leukoencephalopathy: a comparative study with in situ hybridization and polymerase chain reaction. Muñoz-Mármol, A.M., Mola, G., Fernández-Vasalo, A., Vela, E., Mate, J.L., Ariza, A. J. Neuropathol. Exp. Neurol. (2004) [Pubmed]
  21. Cell-free translation of simian virus 40 16S and 19S L-strand-specific mRNA classes to simian virus 40 major VP-1 and minor VP-2 and VP-3 capsid proteins. Prives, C.L., Shure, H. J. Virol. (1979) [Pubmed]
 
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