The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

HpVgp4  -  capsid protein

Hamster polyomavirus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of HpVgp4

  • Chimeric bacteriophage fr virus-like particles harboring the immunodominant C-terminal region of hamster polyomavirus VP1 induce a strong VP1-specific antibody response in rabbits and mice [1].
  • Phage fr coat protein-derived virus-like particles tolerated the N-terminal fusion of amino acids 333-384, 351-384, 351-374, and 364-384, respectively, of VP1 [1].
  • The high flexibility of the C-terminal region of VP1 was confirmed by the formation of chimeric virus-like particles based on the coat protein of the RNA bacteriophage fr which was previously found to tolerate only very short-sized foreign insertions [1].
  • Renaturation of the purified VP1 protein resulted in the formation of subunits that were morphologically, biophysically, and immunologically similar to native virion capsomeres [2].
  • Electron microscopy showed that isolated recombinant VP1 protein self-assembled into a capsid-like structure similar to the natural empty capsid [3].

Psychiatry related information on HpVgp4


High impact information on HpVgp4

  • The 3' on OH terminal G of this segment is part of the G-C-C codeword for the N terminal alanine of the VP1 protein [5].
  • Expression of capsid antigen VP1 ("late gene products") required at least three GGGCGG boxes, sequences between nucleotides 197 and 273 in the 72-bp repeat region, and transactivation by T-Ag [6].
  • The crystal structure of polyoma VP1 with a sialic acid-containing oligosaccharide was used to derive a model of how the two terminal sugars (sialic acid-alpha2,3-galactose) in one branch of GD1a and GT1b are recognized by the virus [7].
  • The ability of mutants such as Py1387T to induce S6 phosphorylation correlated with their ability to increase phosphorylation of VP1, an event linked to maturation of infectious virions [8].
  • CK II phosphorylated VP1 on serine, and the resulting tryptic phosphopeptide eluted in a 30-31 min high performance liquid chromatography fraction corresponding to residues 58-78 [9].

Chemical compound and disease context of HpVgp4

  • Polyomavirus nontransforming host range (hr-t) mutants are defective in VP1 threonine phosphorylation when grown in nonpermissive cells (R. L. Garcea, K. Ballmer-Hofer, and T. L. Benjamin, J. Virol. 54:311-316, 1985) [10].
  • Upon expression in Escherichia coli and purification by immunoaffinity chromatography, wild-type VP1 was isolated as pentameric, capsomere-like structures which could be induced to form capsid-like structures upon addition of CaCl2, consistent with previous studies [11].
  • We investigated whether the VP1 protein of simian virus 40 binds to DNA [12].
  • We used simian virus 40 tsB201 (unable to produce viral capsid at the restrictive temperature of 41 degrees C because of a point mutation in the VP1 gene) to analyze the mutagenic potency of the two major UV-induced lesions, pyrimidine dimers (Py-Py) and pyrimidine (6-4) pyrimidones [Py(6-4)Py], which are formed on the same nucleotide sites [13].
  • The use of a tryptophan promoter-driven Escherichia coli expression system resulted in the efficient synthesis of VP1 and VP1(ext) and formation of VLPs [14].

Biological context of HpVgp4

  • Existing taxonomic classifications of BKV come from conventional DNA sequence alignments based on limited data derived from the VP1 gene [15].
  • The most polymorphic coding region in the viral genome is VP1, but significant variation is also present in the large T-antigen gene, wherein polymorphisms are found in 11.39% of all nucleotide sites, 46.22% of which are cluster specific [15].
  • The sequence information needed for assigning genotypes can be captured by VP1, VP2, VP3, or large T-gene sequencing [15].
  • The double-stranded genome of the small DNA tumor virus, polyomavirus, is enclosed in a capsid composed of a major protein, VP1, which associates as pentameric capsomeres into an icosahedral structure, and two minor proteins, VP2 and VP3, whose functions and positions within the structure are unknown [16].
  • The polyomavirus proteins VP1, VP2, and VP3 move from their cytoplasmic site of synthesis into the nucleus, where virus assembly occurs [17].

Anatomical context of HpVgp4

  • For both groups of hamsters in the C-terminal region of VP1 immunodominant B-cell epitopes were identified in the regions between amino acids 305 and 351 and amino acids 351 and 384 [1].
  • VP1 protein expressed in E. coli self-assembled into capsid-like particles and caused haemagglutination of human O-type red blood cells [18].
  • To identify cellular or viral components which might control this process, we determined the distribution of VP1, VP2, and VP3 in a soluble fraction, a cytoplasmic cytoskeleton fraction, and a nuclear framework fraction of infected cells [17].
  • In addition, production of VP1 protein was observed in the T.wt/BL cell line [19].
  • VP2 and VP3, but not VP1, caused the permeabilization of bacterial membranes [20].

Associations of HpVgp4 with chemical compounds

  • The recombinant production of the VP1 protein offers a save way to obtain a highly purified, non pathogenic pharmaceutical excipient [21].
  • Previous mapping of the in vivo phosphorylation sites on VP1 identified phosphorylation of threonine residues Thr-63 and Thr-156 (Li, M., and Garcea, R. L. (1994) J. Virol. 68, 320-327) [9].
  • However, although VP1 containing the point mutation was isolated as pentamers which were indistinguishable from wild-type VP1 pentamers, addition of CaCl2 did not result in their assembly into capsid-like structures [11].
  • Formic acid cleavage of the 43-kilodalton (kDa) VP1 protein into 29-, 18-, and 16-kDa fragments before 45Ca-binding analysis revealed that only the 18- and 16-kDa carboxyl-terminal fragments of this protein bind 45Ca [22].
  • Phosphoamino acid analysis of 32P-labeled VP1 revealed that phosphoserine is the only phosphoamino acid present in the VP1 protein [23].

Other interactions of HpVgp4

  • In the PCR assay, both early large T antigen (LT) and late (VP1) transcriptional BKV coding regions were found in renal tissue, whereas EBV and only LT-BK were detected in PTLD abdominal tissue [24].

Analytical, diagnostic and therapeutic context of HpVgp4


  1. Chimeric bacteriophage fr virus-like particles harboring the immunodominant C-terminal region of hamster polyomavirus VP1 induce a strong VP1-specific antibody response in rabbits and mice. Voronkova, T., Grosch, A., Kazaks, A., Ose, V., Skrastina, D., Sasnauskas, K., Jandrig, B., Arnold, W., Scherneck, S., Pumpens, P., Ulrich, R. Viral Immunol. (2002) [Pubmed]
  2. Chromatographic separation of the polyoma virus proteins and renaturation of the isolated VP1 major capsid protein. Brady, J.N., Consigli, R.A. J. Virol. (1978) [Pubmed]
  3. 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]
  4. Lack of JC viral genomic sequences in multiple sclerosis brain tissue by polymerase chain reaction. Buckle, G.J., Godec, M.S., Rubi, J.U., Tornatore, C., Major, E.O., Gibbs, C.J., Gajdusek, D.C., Asher, D.M. Ann. Neurol. (1992) [Pubmed]
  5. The initiation region of the SV40 VP1 gene. Van de Voorde, A., Contreras, R., Rogiers, R., Fiers, W. Cell (1976) [Pubmed]
  6. cis- and trans-acting sequences required for expression of simian virus 40 genes in mouse oocytes. Chalifour, L.E., Wirak, D.O., Hansen, U., Wassarman, P.M., DePamphilis, M.L. Genes Dev. (1987) [Pubmed]
  7. Gangliosides are receptors for murine polyoma virus and SV40. Tsai, B., Gilbert, J.M., Stehle, T., Lencer, W., Benjamin, T.L., Rapoport, T.A. EMBO J. (2003) [Pubmed]
  8. Polyomavirus middle T antigen induces ribosomal protein S6 phosphorylation through pp60c-src-dependent and -independent pathways. Talmage, D.A., Blenis, J., Benjamin, T.L. Mol. Cell. Biol. (1988) [Pubmed]
  9. In vitro phosphorylation of the polyomavirus major capsid protein VP1 on serine 66 by casein kinase II. Li, M., Lyon, M.K., Garcea, R.L. J. Biol. Chem. (1995) [Pubmed]
  10. Identification of the threonine phosphorylation sites on the polyomavirus major capsid protein VP1: relationship to the activity of middle T antigen. Li, M., Garcea, R.L. J. Virol. (1994) [Pubmed]
  11. Mutations in the putative calcium-binding domain of polyomavirus VP1 affect capsid assembly. Haynes, J.I., Chang, D., Consigli, R.A. J. Virol. (1993) [Pubmed]
  12. DNA-binding properties of the major structural protein of simian virus 40. Soussi, T. J. Virol. (1986) [Pubmed]
  13. Respective roles of pyrimidine dimer and pyrimidine (6-4) pyrimidone photoproducts in UV mutagenesis of simian virus 40 DNA in mammalian cells. Bourre, F., Benoit, A., Sarasin, A. J. Virol. (1989) [Pubmed]
  14. Hamster polyomavirus-derived virus-like particles are able to transfer in vitro encapsidated plasmid DNA to mammalian cells. Voronkova, T., Kazaks, A., Ose, V., Ozel, M., Scherneck, S., Pumpens, P., Ulrich, R. Virus Genes (2007) [Pubmed]
  15. Phylogenetic analysis of polyomavirus BK sequences. Sharma, P.M., Gupta, G., Vats, A., Shapiro, R., Randhawa, P. J. Virol. (2006) [Pubmed]
  16. Myristylated polyomavirus VP2: role in the life cycle of the virus. Krauzewicz, N., Streuli, C.H., Stuart-Smith, N., Jones, M.D., Wallace, S., Griffin, B.E. J. Virol. (1990) [Pubmed]
  17. Expression of polyomavirus virion proteins by a vaccinia virus vector: association of VP1 and VP2 with the nuclear framework. Stamatos, N.M., Chakrabarti, S., Moss, B., Hare, J.D. J. Virol. (1987) [Pubmed]
  18. The major capsid protein, VP1, of human JC virus expressed in Escherichia coli is able to self-assemble into a capsid-like particle and deliver exogenous DNA into human kidney cells. Ou, W.C., Wang, M., Fung, C.Y., Tsai, R.T., Chao, P.C., Hseu, T.H., Chang, D. J. Gen. Virol. (1999) [Pubmed]
  19. Interference of mouse polyomavirus with the c-myc gene and its product in mouse mammary adenocarcinomas. Holländerová, D., Raslová, H., Blangy, D., Forstová, J., Berebbi, M. Int. J. Oncol. (2003) [Pubmed]
  20. 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]
  21. Recombinant virus like particles as drug delivery system. Georgens, C., Weyermann, J., Zimmer, A. Current pharmaceutical biotechnology. (2005) [Pubmed]
  22. Localization of calcium on the polyomavirus VP1 capsid protein. Ludlow, J.W., Consigli, R.A. J. Virol. (1987) [Pubmed]
  23. Phosphorylation of the budgerigar fledgling disease virus major capsid protein VP1. Haynes, J.I., Consigli, R.A. J. Virol. (1992) [Pubmed]
  24. LT, VP1 and TCR-BKV sequence analysis in a patient with post-transplant BKV nephropathy associated with EBV-related PTLD. Rubio, L., Vera-Sempere, F.J., Moreno-Baylach, M.J., García, A., Zamora, I., Simón, J. Pediatr. Nephrol. (2005) [Pubmed]
  25. 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]
WikiGenes - Universities