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Gene Review

VP1  -  capsid protein

Mouse parvovirus 1

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Disease relevance of VP1

  • In contrast, the predicted amino acid sequence of the capsid proteins of MPV was different from sequences of other parvoviruses [1].
  • To investigate whether a DNA virus can evade passive immunotherapy with a polyclonal antiserum, we analyzed the protection of a neutralizing capsid antiserum against a lethal infection of the immunosuppressive strain of the parvovirus minute virus of mice (MVMi) in 42 immunodeficient mice over a period of 200 days [2].
  • Analysis of parental phH1 virus infection of SW480 colon cancer cells showed that the nonstructural and capsid proteins were expressed, but single stranded DNA and progeny virus were not produced [3].
  • To this end, the major capsid viral protein (VP2) genes of MMV and MPV were cloned and MMV recombinant VP2 (rVP2) and MPV rVP2 proteins were expressed by using a baculovirus system [4].
  • Adeno-Associated Virus Type 2 Capsids with Externalized VP1/VP2 Trafficking Domains Are Generated prior to Passage through the Cytoplasm and Are Maintained until Uncoating Occurs in the Nucleus [5].

High impact information on VP1

  • We have individually truncated by mutation to alanine many (ten) of these side chains and analyzed the effects on capsid assembly, stability and conformation, viral DNA encapsidation, and virion infectivity [6].
  • Low pH-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the VP1 N-terminal sequence (N-VP1), N-VP2 cleavage, and uncoating of the full-length genome [7].
  • Although a fraction of the VP1-containing trimers were translocated into the nucleus driven by the conventional nuclear transport signal of VP1 N terminus, their further assembly in the absence of the VP2-only trimers yielded large molecular mass amorphous aggregates [8].
  • Upon limited heat treatment in vitro, the pores can function as portals to externalize VP1/VP2 protein N-terminal sequences which harbor infection-relevant functional domains, such as a phospholipase A(2) catalytic domain [5].
  • While incubation of cells with bafilomycin A1 reduced exposure of VP1/VP2 N termini, incubation with chloroquine stimulated externalization transiently [5].

Chemical compound and disease context of VP1


Biological context of VP1

  • The pathogenesis of infection with minute virus of mice depends on expression of the small nonstructural protein NS2 and on the genotype of the allotropic determinants VP1 and VP2 [11].
  • We have identified, in the genome of B19, a second transcriptional promoter activity at map position 44, before the capsid protein genes [12].
  • Sequential virus titration, histology, in situ hybridization with a full-length MVMi genomic probe, and immunohistochemistry for viral capsid antigen were used to compare the pathogenesis of infection with the four MVM genotypes [11].
  • The virus was most closely related to bovine parvovirus (BPV), with which it was 43% identical at the DNA sequence level, while the NS1 and VP1 proteins were 33.6 and 41.4% identical to those of BPV, respectively [13].
  • Alternative splicing of capsid gene (VP) transcripts (either 2280-AG/GT or 2313-AG/GT spliced with 2386-AG/GA), to maintain or remove the first AUG (at 2287) in the ORF, yielded two 2.9-kb mRNAs containing a nested set of protein-coding sequences (VP-1 and VP-2 with predicted molecular mass 80.9 and 64.3 kDa, respectively) [14].

Anatomical context of VP1

  • Synthesis of the NS1 nonstructural protein occurs in permissive and nonpermissive cells, such as megakaryocytes, whereas synthesis of the VP1 and VP2 capsid proteins seems to be restricted to burst-forming units and CFU of erythroid cells [15].
  • KBSH, propagated in swine testes cells in culture, possessed two major capsid polypeptides of 83 and 64 kilodaltons that were similar in size to those of PPV [16].
  • Cells resembling lymphocytes and macrophages contained both ADV capsid (VP2) and nonstructural (NS1 and NS2) proteins, and were present in a distribution suggestive of infected cells within germinal centres [17].
  • CONCLUSIONS: B cell memory is established and maintained against conformational epitopes of VP2 and against linear epitopes of VP1 but not against linear epitopes of VP2 [18].
  • Evaluation of ex vivo T cell responses from 149/199 individuals showed significantly higher interferon-gamma levels for seropositive individuals following VP1 (268 +/- 36 versus 103 +/- 19 pg/ml; P = 0.003) and VP2 (242 +/- 42 versus 91 +/- 16 pg/ml; P = 0.01) antigen stimulation [19].

Associations of VP1 with chemical compounds

  • These two protein species comigrated at 110S on neutral sucrose velocity gradients with the B19 viral DNA and thus appear to constitute the viral capsid polypeptides [20].
  • The ability of the mutant proteins to complement a replication defective NS-1 mutant of the infectious MVM plasmid pMM984 and to activate transcription from the capsid gene promoter in chloramphenicol acetyl transferase expression assays was determined [21].
  • The VP1 (82 kDa) and VP2 (63 kDa) proteins forming the T = 1 icosahedral MVM capsid at the respective 1:5 molar ratio of synthesis, could be covalently cross-linked with dimethyl suberimidate into two types of oligomeric assemblies, which were present at stoichiometric amounts in infected cell extracts and purified viral particles [8].
  • When four or more methylene-sized groups were introduced, or six or more groups removed, capsid assembly was drastically impaired [22].
  • Lysine 531 is unique to AAV6 among other known AAV serotypes and is located in a basic cluster near the spikes that surround the icosahedral threefold axes of the AAV capsid [23].

Co-localisations of VP1


Regulatory relationships of VP1


Analytical, diagnostic and therapeutic context of VP1

  • The recombinant baculovirus-expressed ADV VP1 and VP2 showed nuclear localization in Sf9 cells and were able to form particles indistinguishable, by electron microscopy, from wild-type virus [26].
  • Gene therapy vectors have been developed from autonomous rodent parvoviruses that carry a therapeutic gene or a marker gene in place of the genes encoding the capsid proteins [27].
  • In immunoblotting experiments with sera from patients with erythema infectiosum, immunoglobulin G (IgG) and IgM antibodies bound to a single polypeptide of 235 amino acids at the N terminus of VP1 [28].
  • The IgG reactivity was assessed with baculovirus-expressed VP2 or VP1 and VP2 recombinant genotype 1 or genotype 3 proteins in a standardized enzyme immunoassay (EIA) [29].
  • In the IgG Western blot assay, 69 reacted with both VP1 and VP2 and 16 with VP1 only [30].


  1. Molecular characterization of a newly recognized mouse parvovirus. Ball-Goodrich, L.J., Johnson, E. J. Virol. (1994) [Pubmed]
  2. Enhanced cytoplasmic sequestration of the nuclear export receptor CRM1 by NS2 mutations developed in the host regulates parvovirus fitness. López-Bueno, A., Valle, N., Gallego, J.M., Pérez, J., Almendral, J.M. J. Virol. (2004) [Pubmed]
  3. Targeting of autonomous parvoviruses to colon cancer by insertion of Tcf sites in the P4 promoter. Malerba, M., Nikolova, D., Cornelis, J., Iggo, R. Cancer Gene Ther. (2006) [Pubmed]
  4. Serodiagnosis of mice minute virus and mouse parvovirus infections in mice by enzyme-linked immunosorbent assay with baculovirus-expressed recombinant VP2 proteins. Livingston, R.S., Besselsen, D.G., Steffen, E.K., Besch-Williford, C.L., Franklin, C.L., Riley, L.K. Clin. Diagn. Lab. Immunol. (2002) [Pubmed]
  5. Adeno-Associated Virus Type 2 Capsids with Externalized VP1/VP2 Trafficking Domains Are Generated prior to Passage through the Cytoplasm and Are Maintained until Uncoating Occurs in the Nucleus. Sonntag, F., Bleker, S., Leuchs, B., Fischer, R., Kleinschmidt, J.A. J. Virol. (2006) [Pubmed]
  6. Functional relevance of amino acid residues involved in interactions with ordered nucleic acid in a spherical virus. Reguera, J., Grueso, E., Carreira, A., Sánchez-Martínez, C., Almendral, J.M., Mateu, M.G. J. Biol. Chem. (2005) [Pubmed]
  7. Low pH-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the VP1 N-terminal sequence (N-VP1), N-VP2 cleavage, and uncoating of the full-length genome. Mani, B., Baltzer, C., Valle, N., Almendral, J.M., Kempf, C., Ros, C. J. Virol. (2006) [Pubmed]
  8. Nuclear transport of trimeric assembly intermediates exerts a morphogenetic control on the icosahedral parvovirus capsid. Riolobos, L., Reguera, J., Mateu, M.G., Almendral, J.M. J. Mol. Biol. (2006) [Pubmed]
  9. Phosphorylation status of the parvovirus minute virus of mice particle: mapping and biological relevance of the major phosphorylation sites. Maroto, B., Ramírez, J.C., Almendral, J.M. J. Virol. (2000) [Pubmed]
  10. Structure comparisons of Aedes albopictus densovirus with other parvoviruses. Cheng, L., Chen, S., Zhou, Z.H., Zhang, J. Sci. China, C, Life Sci. (2007) [Pubmed]
  11. The pathogenesis of infection with minute virus of mice depends on expression of the small nonstructural protein NS2 and on the genotype of the allotropic determinants VP1 and VP2. Brownstein, D.G., Smith, A.L., Johnson, E.A., Pintel, D.J., Naeger, L.K., Tattersall, P. J. Virol. (1992) [Pubmed]
  12. Nonstructural protein of parvoviruses B19 and minute virus of mice controls transcription. Doerig, C., Hirt, B., Antonietti, J.P., Beard, P. J. Virol. (1990) [Pubmed]
  13. The canine minute virus (minute virus of canines) is a distinct parvovirus that is most similar to bovine parvovirus. Schwartz, D., Green, B., Carmichael, L.E., Parrish, C.R. Virology (2002) [Pubmed]
  14. Genomic organization and mapping of transcription and translation products of the NADL-2 strain of porcine parvovirus. Bergeron, J., Menezes, J., Tijssen, P. Virology (1993) [Pubmed]
  15. The 3' untranslated region of the B19 parvovirus capsid protein mRNAs inhibits its own mRNA translation in nonpermissive cells. Pallier, C., Greco, A., Le Junter, J., Saib, A., Vassias, I., Morinet, F. J. Virol. (1997) [Pubmed]
  16. KBSH parvovirus: comparison with porcine parvovirus. Molitor, T.W., Joo, H.S., Collett, M.S. J. Virol. (1985) [Pubmed]
  17. Replication of Aleutian mink disease parvovirus in mink lymph node histocultures. Jensen, K.T., Wolfinbarger, J.B., Aasted, B., Bloom, M.E. J. Gen. Virol. (2000) [Pubmed]
  18. B cell memory is directed toward conformational epitopes of parvovirus B19 capsid proteins and the unique region of VP1. Corcoran, A., Mahon, B.P., Doyle, S. J. Infect. Dis. (2004) [Pubmed]
  19. Ex vivo cytokine responses against parvovirus B19 antigens in previously infected pregnant women. Corcoran, A., Mahon, B.P., McParland, P., Davoren, A., Doyle, S. J. Med. Virol. (2003) [Pubmed]
  20. Identification of the major structural and nonstructural proteins encoded by human parvovirus B19 and mapping of their genes by procaryotic expression of isolated genomic fragments. Cotmore, S.F., McKie, V.C., Anderson, L.J., Astell, C.R., Tattersall, P. J. Virol. (1986) [Pubmed]
  21. Characterization of linker insertion and point mutations in the NS-1 gene of minute virus of mice: effects on DNA replication and transcriptional activation functions of NS-1. Skiadopoulos, M.H., Salvino, R., Leong, W.L., Faust, E.A. Virology (1992) [Pubmed]
  22. Structural tolerance versus functional intolerance to mutation of hydrophobic core residues surrounding cavities in a parvovirus capsid. Carreira, A., Mateu, M.G. J. Mol. Biol. (2006) [Pubmed]
  23. Single amino Acid changes can influence titer, heparin binding, and tissue tropism in different adeno-associated virus serotypes. Wu, Z., Asokan, A., Grieger, J.C., Govindasamy, L., Agbandje-McKenna, M., Samulski, R.J. J. Virol. (2006) [Pubmed]
  24. The autonomous parvovirus MVM encodes two nonstructural proteins in addition to its capsid polypeptides. Cotmore, S.F., Sturzenbecker, L.J., Tattersall, P. Virology (1983) [Pubmed]
  25. Characterization of the trans-activation-responsive element of the parvovirus H-1 P38 promoter. Rhode, S.L., Richard, S.M. J. Virol. (1987) [Pubmed]
  26. Expression of Aleutian mink disease parvovirus proteins in a baculovirus vector system. Christensen, J., Storgaard, T., Bloch, B., Alexandersen, S., Aasted, B. J. Virol. (1993) [Pubmed]
  27. The infectivity and lytic activity of minute virus of mice wild-type and derived vector particles are strikingly different. Lang, S.I., Boelz, S., Stroh-Dege, A.Y., Rommelaere, J., Dinsart, C., Cornelis, J.J. J. Virol. (2005) [Pubmed]
  28. Prokaryotic expression of a VP1 polypeptide antigen for diagnosis by a human parvovirus B19 antibody enzyme immunoassay. Söderlund, M., Brown, K.E., Meurman, O., Hedman, K. J. Clin. Microbiol. (1992) [Pubmed]
  29. Reactivity of genotype-specific recombinant proteins of human erythrovirus B19 with plasmas from areas where genotype 1 or 3 is endemic. Parsyan, A., Kerr, S., Owusu-Ofori, S., Elliott, G., Allain, J.P. J. Clin. Microbiol. (2006) [Pubmed]
  30. Undenatured parvovirus B19 antigens are essential for the accurate detection of parvovirus B19 IgG. Kerr, S., O'Keeffe, G., Kilty, C., Doyle, S. J. Med. Virol. (1999) [Pubmed]
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