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Gene Review

VP1  -  Major capsid protein VP1

Murine pneumotropic virus

 
 
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Disease relevance of VP1

  • Location of the sequences coding for capsid proteins VP1 and VP2 on polyoma virus DNA [1].
  • Comparison of the chain lengths of the capsid proteins with the size of the viral mRNAs coding for them suggests that VP1 and VP2 are entirely virus-coded [1].
  • Coproduction of the capsid proteins VP1, VP2, and VP3 was achieved by infecting Sf9 cells with the three recombinant baculovirus species at equal multiplicities [2].
  • This result indicates that some of the disulfide bonds bridging the VP1 proteins are on the virion surface [3].
  • Analysis of capsid formation of human polyomavirus JC (Tokyo-1 strain) by a eukaryotic expression system: splicing of late RNAs, translation and nuclear transport of major capsid protein VP1, and capsid assembly [4].
 

High impact information on VP1

  • Here we report the results of transfection of COS-7 cells with an SV40 expression vector containing preprosomatostatin cDNA cloned into the VP-1 late gene [5].
  • Overlapping of the VP2-VP3 gene and the VP1 gene in the SV40 genome [6].
  • The 16S RNA codes only for polyoma capsid protein VP1, while the 19S RNA codes in addition for capsid protein VP2 [1].
  • Since the 19S and 16S species have been previously mapped on the viral genome, these results allow us to deduce the location of the sequences coding for VP1 and VP2 [1].
  • A domain of SV40 capsid polypeptide VP1 that specifies migration into the cell nucleus [7].
 

Chemical compound and disease context of VP1

 

Biological context of VP1

  • Existing taxonomic classifications of BKV come from conventional DNA sequence alignments based on limited data derived from the VP1 gene [13].
  • The sequence information needed for assigning genotypes can be captured by VP1, VP2, VP3, or large T-gene sequencing [13].
  • Mutation analysis indicated that inefficiency in nuclear transport of VP1 is due to the unique structure in the N-terminal sequence, KRKGERK [4].
  • The presence of the open reading frame of the agnoprotein or the leader sequence (nucleotides 275 to 409) can decrease the expression level of VP1 [4].
  • Truncation of the nuclear localization signal of polyomavirus VP1 results in a loss of DNA packaging when expressed in the baculovirus system [14].
 

Anatomical context of VP1

 

Associations of VP1 with chemical compounds

  • When VP1 was coexpressed with VP2, the nonphysiologic serine phosphorylation of VP1 was decreased, and a tryptic peptide containing Thr-63, a site modified during virus infection of mouse cells, was phosphorylated [9].
  • Polyoma mRNA species have been isolated by preparative hybridization to purified viral DNA immobilized on cellulose nitrate filters and shown to code for both VP1 and VP2 [10].
  • VP1, VP2, and vp3 were all labeled with [35S] formylmethionine when they were synthesized in the presence of [35S] formylmethionyl-tRNAfmet [20].
  • The presence of the first 11 NH2-terminal amino acids from SV40 VP1 was found to be sufficient to target the fusion protein to the cell nucleus [7].
  • Seven of the antibodies reacted with denatured VP1 and also recognized fragments generated by protease or cyanogen bromide cleavage [21].
 

Physical interactions of VP1

  • Recombinant VP1 coimmunoprecipitated with recombinant VP2 or truncated VP2 (delta C12VP2), which lacked the carboxy-terminal 12 amino acids [22].
 

Other interactions of VP1

  • When antibody against viral capsid protein Vp1 or Vp3 was introduced into the cytoplasm, the nuclear accumulation of T antigen was not observed in cells either infected or cytoplasmically injected with virion [23].
 

Analytical, diagnostic and therapeutic context of VP1

  • Immunoprecipitation of lysates from co-infected cells demonstrated an association between VP1 and VP2 [24].
  • Amplification by PCR and sequencing detected VP1 -encoding sequences showing a high degree of homology with HaPV [25].
  • Using recombinant major capsid protein VP1 of HaPV, VP1-specific antibodies were detected in sera from 12 of 12 affected hamsters and in four of four unaffected in-contact hamsters, by ELISA [25].
  • This protein-protein interaction was substantiated by laser scanning confocal microscopy of Sf9 cells that were co-infected with VP1, VP2 and VP3 recombinant viruses [16].
  • Maximum homologies appear to occur in the regions which code for the C-terminal of VP1, on the contrary of the result of heteroduplex analysis 6 with 6 with SV40 and polyoma virus DNAs [26].

References

  1. Location of the sequences coding for capsid proteins VP1 and VP2 on polyoma virus DNA. Smith, A.E., Kamen, R., Mangel, W.F., Shure, H., Wheeler, T. Cell (1976) [Pubmed]
  2. Self-assembly and protein-protein interactions between the SV40 capsid proteins produced in insect cells. Sandalon, Z., Oppenheim, A. Virology (1997) [Pubmed]
  3. Simian virus 40 chromatin interaction with the capsid proteins. Bina, M., Ng, S.C., Blasquez, V. J. Biomol. Struct. Dyn. (1983) [Pubmed]
  4. Analysis of capsid formation of human polyomavirus JC (Tokyo-1 strain) by a eukaryotic expression system: splicing of late RNAs, translation and nuclear transport of major capsid protein VP1, and capsid assembly. Shishido-Hara, Y., Hara, Y., Larson, T., Yasui, K., Nagashima, K., Stoner, G.L. J. Virol. (2000) [Pubmed]
  5. Expression of preprosomatostatin in heterologous cells: biosynthesis, posttranslational processing, and secretion of mature somatostatin. Warren, T.G., Shields, D. Cell (1984) [Pubmed]
  6. Overlapping of the VP2-VP3 gene and the VP1 gene in the SV40 genome. Contreras, R., Rogiers, R., Van de Voorde, A., Fiers, W. Cell (1977) [Pubmed]
  7. A domain of SV40 capsid polypeptide VP1 that specifies migration into the cell nucleus. Wychowski, C., Benichou, D., Girard, M. EMBO J. (1986) [Pubmed]
  8. Conformational changes of murine polyomavirus capsid proteins induced by sialic acid binding. Cavaldesi, M., Caruso, M., Sthandier, O., Amati, P., Garcia, M.I. J. Biol. Chem. (2004) [Pubmed]
  9. Polyomavirus VP1 phosphorylation: coexpression with the VP2 capsid protein modulates VP1 phosphorylation in Sf9 insect cells. Li, M., Delos, S.E., Montross, L., Garcea, R.L. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  10. Cell-free synthesis of polyoma virus capsid proteins VP1 and VP2. Wheeler, T., Bayley, S.T., Harvey, R., Crawford, L.V., Smith, A.E. J. Virol. (1977) [Pubmed]
  11. Proteins in intracellular simian virus 40 nucleoportein complexes: comparison with simian virus 40 core proteins. Meinke, W., Hall, M.R., Goldstein, D.A. J. Virol. (1975) [Pubmed]
  12. Alpha4beta1 integrin acts as a cell receptor for murine polyomavirus at the postattachment level. Caruso, M., Belloni, L., Sthandier, O., Amati, P., Garcia, M.I. J. Virol. (2003) [Pubmed]
  13. Phylogenetic analysis of polyomavirus BK sequences. Sharma, P.M., Gupta, G., Vats, A., Shapiro, R., Randhawa, P. J. Virol. (2006) [Pubmed]
  14. Truncation of the nuclear localization signal of polyomavirus VP1 results in a loss of DNA packaging when expressed in the baculovirus system. Gillock, E.T., An, K., Consigli, R.A. Virus Res. (1998) [Pubmed]
  15. 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]
  16. Avian polyomavirus major capsid protein VP1 interacts with the minor capsid proteins and is transported into the cell nucleus but does not assemble into capsid-like particles when expressed in the baculovirus system. An, K., Smiley, S.A., Gillock, E.T., Reeves, W.M., Consigli, R.A. Virus Res. (1999) [Pubmed]
  17. Efficient intracellular delivery of a protein and a low molecular weight substance via recombinant polyomavirus-like particles. Abbing, A., Blaschke, U.K., Grein, S., Kretschmar, M., Stark, C.M., Thies, M.J., Walter, J., Weigand, M., Woith, D.C., Hess, J., Reiser, C.O. J. Biol. Chem. (2004) [Pubmed]
  18. Concomitant progressive multifocal leucoencephalopathy and primary central nervous system lymphoma expressing JC virus oncogenic protein, large T antigen. Gallia, G.L., DelValle, L., Laine, C., Curtis, M., Khalili, K. MP, Mol. Pathol. (2001) [Pubmed]
  19. Host range transforming gene of polyoma virus plays a role in virus assembly. Garcea, R.L., Benjamin, T.L. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  20. Characterization of the mRNA's for the polyoma virus capsid proteins VP1, VP2, and VP3. Hunter, T., Gibson, W. J. Virol. (1978) [Pubmed]
  21. Epitopes on the major capsid protein of simian virus 40. Babé, L.M., Brew, K., Matsuura, S.E., Scott, W.A. J. Biol. Chem. (1989) [Pubmed]
  22. Expression and purification of recombinant polyomavirus VP2 protein and its interactions with polyomavirus proteins. Cai, X., Chang, D., Rottinghaus, S., Consigli, R.A. J. Virol. (1994) [Pubmed]
  23. Association with capsid proteins promotes nuclear targeting of simian virus 40 DNA. Nakanishi, A., Clever, J., Yamada, M., Li, P.P., Kasamatsu, H. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  24. Expression of the polyomavirus VP2 and VP3 proteins in insect cells: coexpression with the major capsid protein VP1 alters VP2/VP3 subcellular localization. Delos, S.E., Montross, L., Moreland, R.B., Garcea, R.L. Virology (1993) [Pubmed]
  25. Polyomavirus infection in hamsters and trichoepitheliomas/cutaneous adnexal tumours. Foster, A.P., Brown, P.J., Jandrig, B., Grosch, A., Voronkova, T., Scherneck, S., Ulrich, R. Vet. Rec. (2002) [Pubmed]
  26. The primary sequence of the late region of polyoma virus DNA II. The expression of the late genes and comparison with DNA sequences of SV40 and BKV. Soeda, E. Nucleic Acids Symp. Ser. (1979) [Pubmed]
 
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