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

PestiV2gp1  -  polyprotein

Classical swine fever virus

 
 
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 PestiV2gp1

 

High impact information on PestiV2gp1

 

Chemical compound and disease context of PestiV2gp1

  • Classical swine fever virus (CSFV) E2 glycoprotein contains a discrete epitope (TAVSPTTLR, residues 829-837 of CSFV polyprotein) recognized by monoclonal antibody (mAb) WH303, used to differentiate CSFV from related ruminant pestiviruses, Bovine Viral Diarrhea Virus (BVDV) and Border Disease Virus (BDV), that infect swine without causing disease [8].
 

Biological context of PestiV2gp1

  • We have analyzed the structural role of polyprotein pp62, the precursor form of mature products p35 and p15, in virus morphogenesis [6].
  • This proteolytic processing was found to take place at the consensus sequence Gly-Gly-X through an ordered cascade of proteolytic cleavages like that which also occurs with ASFV polyprotein pp220 (C. Simón-Mateo, G. Andrés, and E. Viñuela, EMBO J. 12:2977-2987, 1993) [7].
  • It is composed of a 373-nt 5' terminal non-translated region (NTR), a 11697-nt open reading frame (ORF) encoding a polyprotein of 3898 amino acids (aa), and a 226-nt 3'-NTR [9].
 

Anatomical context of PestiV2gp1

  • At the electron microscopic level, antibodies to pp220 labeled all identifiable forms of the virus from the precursor viral membranes onward, thus indicating an early role of the polyprotein pp220 in ASFV assembly [2].
  • The single best-defined, SLA-I restricted porcine CD8(+) T-cell epitope currently known is a 9-residue peptide from the polyprotein of CSFV (J. Gen. Virol. 76 (1995) 3039) [10].
 

Analytical, diagnostic and therapeutic context of PestiV2gp1

  • Immunoelectron microscopy revealed that the pp62-derived products localize at the core shell, a matrix-like domain placed between the DNA-containing nucleoid and the inner envelope, where the pp220-derived products are also localized [6].
  • Immunofluorescence studies showed that polyprotein pp62 is localized in the viral factories [7].
  • Electron microscopy revealed that pp220 repression leads to the assembly of icosahedral particles virtually devoid of the core structure [5].
  • Analysis of recombinant v220i by immunoelectron microscopy, immunoblotting, and DNA hybridization showed that mutant particles essentially lack, besides the pp220-derived products, a number of major core proteins as well as the viral DNA [5].
  • Furthermore, the use of polyprotein pp62 in an ELISA for testing poorly preserved sera allows performance of the diagnosis of ASF without the need to confirm the results by the immunoblot test [11].

References

  1. Polyprotein processing in African swine fever virus: a novel gene expression strategy for a DNA virus. Simón-Mateo, C., Andrés, G., Viñuela, E. EMBO J. (1993) [Pubmed]
  2. Assembly of African swine fever virus: role of polyprotein pp220. Andrés, G., Simón-Mateo, C., Viñuela, E. J. Virol. (1997) [Pubmed]
  3. Cell-derived sequences in the N-terminal region of the polyprotein of a cytopathogenic pestivirus. Müller, A., Rinck, G., Thiel, H.J., Tautz, N. J. Virol. (2003) [Pubmed]
  4. African swine fever virus protease, a new viral member of the SUMO-1-specific protease family. Andrés, G., Alejo, A., Simón-Mateo, C., Salas, M.L. J. Biol. Chem. (2001) [Pubmed]
  5. Repression of African swine fever virus polyprotein pp220-encoding gene leads to the assembly of icosahedral core-less particles. Andrés, G., García-Escudero, R., Salas, M.L., Rodríguez, J.M. J. Virol. (2002) [Pubmed]
  6. African swine fever virus polyproteins pp220 and pp62 assemble into the core shell. Andrés, G., Alejo, A., Salas, J., Salas, M.L. J. Virol. (2002) [Pubmed]
  7. Proteolytic processing in African swine fever virus: evidence for a new structural polyprotein, pp62. Simón-Mateo, C., Andrés, G., Almazán, F., Viñuela, E. J. Virol. (1997) [Pubmed]
  8. Identification of a novel virulence determinant within the E2 structural glycoprotein of classical swine fever virus. Risatti, G.R., Holinka, L.G., Carrillo, C., Kutish, G.F., Lu, Z., Tulman, E.R., Sainz, I.F., Borca, M.V. Virology (2006) [Pubmed]
  9. Genome comparison of a novel classical swine fever virus isolated in China in 2004 with other CSFV strains. Li, X., Xu, Z., He, Y., Yao, Q., Zhang, K., Jin, M., Chen, H., Qian, P. Virus Genes (2006) [Pubmed]
  10. Development of a rapid in vitro protein refolding assay which discriminates between peptide-bound and peptide-free forms of recombinant porcine major histocompatibility class I complex (SLA-I). Oleksiewicz, M.B., Kristensen, B., Ladekjaer-Mikkelsen, A.S., Nielsen, J. Vet. Immunol. Immunopathol. (2002) [Pubmed]
  11. Antigenic properties and diagnostic potential of African swine fever virus protein pp62 expressed in insect cells. Gallardo, C., Blanco, E., Rodríguez, J.M., Carrascosa, A.L., Sanchez-Vizcaino, J.M. J. Clin. Microbiol. (2006) [Pubmed]
 
WikiGenes - Universities