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Gene Review

VP2  - 

Canine parvovirus

 
 
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Disease relevance of VP2

  • VP2 gene of a canine parvovirus isolate from stool of a puppy [1].
  • We report the insertion of oligonucleotides coding for a short linear epitope from the VP2 capsid protein of mink enteritis virus (MEV) into an infectious cDNA clone of cowpea mosaic virus and the successful expression of the epitope on the surface of CVPs when propagated in the black-eyed bean, Vigna unguiculata [2].
  • Canine parvovirus capsids are composed of 60 copies of VP2 and 6 to 10 copies of VPl [3].
  • To locate essential sites of interaction between VP2 monomers, we have analyzed the effects of a number of VP2 deletion mutants representing the amino terminus and the four major loops of the surface, using as an assay the formation of virus-like particles (VLPs) expressed by recombinant baculoviruses [3].
  • The recombinant VP2 shows also the capability to self-assemble, forming viruslike particles similar in size and appearance to CPV virions [4].
 

High impact information on VP2

  • These regions were compared in the CPV and FPV capsid structures that have been determined, as well as in two new structures of CPV capsids that contain substitutions of the VP2 Asn-93 to Asp and Arg, respectively [5].
  • The three-dimensional structure of expressed VP2 capsids of Aleutian mink disease parvovirus strain G (ADVG-VP2) has been determined to 22 A resolution by cryo-electron microscopy and image reconstruction techniques [6].
  • Three other mutants whose genomes contain mutations which affect one probable interchain bond were nonviable and could not be propagated in either canine or feline cells, although the VP1 and VP2 proteins from those mutants produced empty capsids when expressed from a plasmid vector [7].
  • Peptide vaccine against canine parvovirus: identification of two neutralization subsites in the N terminus of VP2 and optimization of the amino acid sequence [8].
  • Within the N-terminal 23 residues of VP2, two subsites able to induce neutralizing antibodies and which overlapped by only two glycine residues at positions 10 and 11 could be discriminated [8].
 

Chemical compound and disease context of VP2

 

Biological context of VP2

  • An immunodominant region on baculovirus-produced parvovirus B19 VP2 capsids was localized between amino acids 259 and 426 by mapping the binding sites of a panel of monoclonal antibodies which recognize determinants on the particles [11].
  • The CPV variants selected by cloning the VP2 gene were sequenced, and genetic diversity and selection pressure were investigated [12].
  • However, only insertions of the C3:B epitope in VP2 residue 225 of the loop 2 were able to elicit a significant anti-peptide antibody response, but not poliovirus-neutralizing antibodies, probably because residue 225 is located in an small depression of the surface [13].
  • Expression of the VP2 DNA was regulated by the vaccinia virus late promoter P11 [14].
  • An infectious raccoon poxvirus (RCNV) was used to express the feline panleukopenia virus (FPV) open reading frame VP2 [14].
 

Anatomical context of VP2

  • VP2 gene of a canine parvovirus (CPV) isolate from the feces of a puppy which was diagnosed to be CPV infection was analysed [1].
  • Proliferative responses of peripheral blood mononuclear cells (PBMC) from CPV-immunized dogs upon stimulation with these and other peptides, covering the major part of the sequence of VP2', identified the presence of T cell epitopes for this species [15].
  • In hemagglutination assay, the expression level of VP2 were 3.2 x 10(3) HA units/ml from infected Bm5 cells, 2.1x 10(5) HA units/larvae from infected larval fat body, and 1.6x 10(6) HA units/ml from infected larval hemolymph [16].
 

Associations of VP2 with chemical compounds

  • The mutation was a single Arg-Lys difference of VP2 amino acid residue 377 [17].
  • Mice and rabbits that received protein-enriched leaf extracts by parenteral route produced high titers of anti-2L21 antibodies able to recognize the VP2 protein [18].
  • The natural cleavage of VP2 to VP3 in CPV full (DNA containing) particles recovered from tissue culture occurred within the sequence Arg-Asn-Glu-Arg Ala-Thr [19].
  • Two Laue diffraction images of HRV14 with a point mutation were sufficient to determine the change from a leucine to a valine in VP2 [20].
 

Other interactions of VP2

 

Analytical, diagnostic and therapeutic context of VP2

References

  1. VP2 gene of a canine parvovirus isolate from stool of a puppy. Hirayama, K., Kano, R., Hosokawa-Kanai, T., Tuchiya, K., Tsuyama, S., Nakamura, Y., Sasaki, Y., Hasegawa, A. J. Vet. Med. Sci. (2005) [Pubmed]
  2. Plant-derived vaccine protects target animals against a viral disease. Dalsgaard, K., Uttenthal, A., Jones, T.D., Xu, F., Merryweather, A., Hamilton, W.D., Langeveld, J.P., Boshuizen, R.S., Kamstrup, S., Lomonossoff, G.P., Porta, C., Vela, C., Casal, J.I., Meloen, R.H., Rodgers, P.B. Nat. Biotechnol. (1997) [Pubmed]
  3. Identification of domains in canine parvovirus VP2 essential for the assembly of virus-like particles. Hurtado, A., Rueda, P., Nowicky, J., Sarraseca, J., Casal, J.I. J. Virol. (1996) [Pubmed]
  4. Recombinant vaccine for canine parvovirus in dogs. López de Turiso, J.A., Cortés, E., Martínez, C., Ruiz de Ybáñez, R., Simarro, I., Vela, C., Casal, I. J. Virol. (1992) [Pubmed]
  5. Structures of host range-controlling regions of the capsids of canine and feline parvoviruses and mutants. Govindasamy, L., Hueffer, K., Parrish, C.R., Agbandje-McKenna, M. J. Virol. (2003) [Pubmed]
  6. Three-dimensional structure of Aleutian mink disease parvovirus: implications for disease pathogenicity. McKenna, R., Olson, N.H., Chipman, P.R., Baker, T.S., Booth, T.F., Christensen, J., Aasted, B., Fox, J.M., Bloom, M.E., Wolfinbarger, J.B., Agbandje-McKenna, M. J. Virol. (1999) [Pubmed]
  7. Canine parvovirus host range is determined by the specific conformation of an additional region of the capsid. Parker, J.S., Parrish, C.R. J. Virol. (1997) [Pubmed]
  8. Peptide vaccine against canine parvovirus: identification of two neutralization subsites in the N terminus of VP2 and optimization of the amino acid sequence. Casal, J.I., Langeveld, J.P., Cortés, E., Schaaper, W.W., van Dijk, E., Vela, C., Kamstrup, S., Meloen, R.H. J. Virol. (1995) [Pubmed]
  9. Structural analysis of a mutation in canine parvovirus which controls antigenicity and host range. Llamas-Saiz, A.L., Agbandje-McKenna, M., Parker, J.S., Wahid, A.T., Parrish, C.R., Rossmann, M.G. Virology (1996) [Pubmed]
  10. Raccoon poxvirus live recombinant feline panleukopenia virus VP2 and rabies virus glycoprotein bivalent vaccine. Hu, L., Ngichabe, C., Trimarchi, C.V., Esposito, J.J., Scott, F.W. Vaccine (1997) [Pubmed]
  11. Localization of an immunodominant domain on baculovirus-produced parvovirus B19 capsids: correlation to a major surface region on the native virus particle. Brown, C.S., Jensen, T., Meloen, R.H., Puijk, W., Sugamura, K., Sato, H., Spaan, W.J. J. Virol. (1992) [Pubmed]
  12. High genetic diversity of the VP2 gene of a canine parvovirus strain detected in a domestic cat. Battilani, M., Scagliarini, A., Ciulli, S., Morganti, L., Prosperi, S. Virology (2006) [Pubmed]
  13. Minor displacements in the insertion site provoke major differences in the induction of antibody responses by chimeric parvovirus-like particles. Rueda, P., Hurtado, A., del Barrio, M., Martínez-Torrecuadrada, J.L., Kamstrup, S., Leclerc, C., Casal, J.I. Virology (1999) [Pubmed]
  14. Raccoon poxvirus feline panleukopenia virus VP2 recombinant protects cats against FPV challenge. Hu, L., Esposito, J.J., Scott, F.W. Virology (1996) [Pubmed]
  15. Delineation of canine parvovirus T cell epitopes with peripheral blood mononuclear cells and T cell clones from immunized dogs. Rimmelzwaan, G.F., Poelen, M.C., Meloen, R.H., Carlson, J., UytdeHaag, F.G., Osterhaus, A.D. J. Gen. Virol. (1990) [Pubmed]
  16. High-level expression of canine parvovirus VP2 using Bombyx mori nucleopolyhedrovirus vector. Choi, J.Y., Woo, S.D., Lee, H.K., Hong, H.K., Je, Y.H., Park, J.H., Song, J.Y., An, S.H., Kang, S.K. Arch. Virol. (2000) [Pubmed]
  17. Mutations adjacent to the dimple of the canine parvovirus capsid structure affect sialic acid binding. Barbis, D.P., Chang, S.F., Parrish, C.R. Virology (1992) [Pubmed]
  18. Induction of neutralizing antibodies by a tobacco chloroplast-derived vaccine based on a B cell epitope from canine parvovirus. Molina, A., Veramendi, J., Hervás-Stubbs, S. Virology (2005) [Pubmed]
  19. Assaying for structural variation in the parvovirus capsid and its role in infection. Weichert, W.S., Parker, J.S., Wahid, A.T., Chang, S.F., Meier, E., Parrish, C.R. Virology (1998) [Pubmed]
  20. Laue diffraction studies of human rhinovirus 14 and canine parvovirus. Hadfield, A., Hajdu, J., Chapman, M.S., Rossmann, M.G. Acta Crystallogr. D Biol. Crystallogr. (1995) [Pubmed]
  21. Tropic determinant for canine parvovirus and feline panleukopenia virus functions through the capsid protein VP2. Spitzer, A.L., Parrish, C.R., Maxwell, I.H. J. Gen. Virol. (1997) [Pubmed]
  22. Expression and subcellular targeting of canine parvovirus capsid proteins in baculovirus-transduced NLFK cells. Gilbert, L., Välilehto, O., Kirjavainen, S., Tikka, P.J., Mellett, M., Käpylä, P., Oker-Blom, C., Vuento, M. FEBS Lett. (2005) [Pubmed]
  23. Rapid method utilizing the polymerase chain reaction for detection of canine parvovirus in feces of diarrheic dogs. Uwatoko, K., Sunairi, M., Nakajima, M., Yamaura, K. Vet. Microbiol. (1995) [Pubmed]
  24. Real-time reverse transcription polymerase chain reaction assay to detect a broad range of feline calicivirus isolates. Wilhelm, S., Truyen, U. J. Virol. Methods (2006) [Pubmed]
  25. Subunit interaction in B19 parvovirus empty capsids. Rosenfeld, S.J., Young, N.S., Alling, D., Ayub, J., Saxinger, C. Arch. Virol. (1994) [Pubmed]
  26. Sequence analysis of VP2 gene of canine parvovirus isolated from domestic dogs in Japan in 1999 and 2000. Doki, M., Fujita, K., Miura, R., Yoneda, M., Ishikawa, Y., Taneno, A., Kai, C. Comp. Immunol. Microbiol. Infect. Dis. (2006) [Pubmed]
 
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