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Gene Review

PRRSVgp5  -  GP4

Porcine reproductive and respiratory syndrome virus

 
 
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Disease relevance of PRRSVgp5

  • Antibodies specific for GP3 and GP4 were detected by a Western immunoblotting assay in swine serum after an infection with Lelystad virus [1].
  • A panel of 15 neutralizing monoclonal antibodies (MAbs) reacted with the native GP4 protein expressed by LV and the recombinant GP4 protein expressed in a Semliki Forest virus expression system [2].
  • The porcine reproductive and respiratory syndrome virus (PRRSV) GP4 and GP5 proteins are two membrane-associated viral glycoproteins that have been shown to induce neutralizing antibodies [3].
  • The expression products of ORFs 2 and 4 are also incorporated into virus particles as additional minor membrane-associated glycoproteins designated as GP2 and GP4, with M(r) of 29 and 31 kDa, respectively [4].
 

High impact information on PRRSVgp5

  • Virions of porcine reproductive and respiratory syndrome virus (PRRSV) contain six membrane proteins: the major proteins GP5 and M and the minor proteins GP2a, E, GP3, and GP4 [5].
  • Comparison of the amino acid sequences of GP4 proteins from various European and North American isolates indicated that the neutralization domain spanning amino acids 40 to 79 is the most variable region of GP4 [2].
  • We propose that the 45- to 50-kDa and 31- to 35-kDa structural proteins of Lelystad virus be named GP3 and GP4, to reflect their glycosylation and the ORFs from which they are expressed [1].
  • To rescue the replication-defective PRRSV, two complementing cell lines, MARC-2000 and MARC-400, were established to stably express the PRRSV GP2 and GP4 proteins, respectively [6].
  • The GP4 also possesses antigenic determinants that trigger the immune system to produce neutralizing antibodies [4].
 

Biological context of PRRSVgp5

  • Using the full-length infectious cDNA clone of North American PRRS isolate P129, the ORF2 and ORF4 genes (which encoded minor structural glycoproteins GP2a/2b and GP4, respectively) were individually deleted from the viral genome [6].
 

Analytical, diagnostic and therapeutic context of PRRSVgp5

  • Reactivity patterns of the MAbs with PRRSV field isolates tested by fixed-cell ELISA showed that there are antigenic variations in PRRSV GP4 and GP5 proteins [7].

References

  1. Proteins encoded by open reading frames 3 and 4 of the genome of Lelystad virus (Arteriviridae) are structural proteins of the virion. van Nieuwstadt, A.P., Meulenberg, J.J., van Essen-Zanbergen, A., Petersen-den Besten, A., Bende, R.J., Moormann, R.J., Wensvoort, G. J. Virol. (1996) [Pubmed]
  2. Posttranslational processing and identification of a neutralization domain of the GP4 protein encoded by ORF4 of Lelystad virus. Meulenberg, J.J., van Nieuwstadt, A.P., van Essen-Zandbergen, A., Langeveld, J.P. J. Virol. (1997) [Pubmed]
  3. Differential host cell gene expression regulated by the porcine reproductive and respiratory syndrome virus GP4 and GP5 glycoproteins. Lee, C., Bachand, A., Murtaugh, M.P., Yoo, D. Vet. Immunol. Immunopathol. (2004) [Pubmed]
  4. Current knowledge on the structural proteins of porcine reproductive and respiratory syndrome (PRRS) virus: comparison of the North American and European isolates. Dea, S., Gagnon, C.A., Mardassi, H., Pirzadeh, B., Rogan, D. Arch. Virol. (2000) [Pubmed]
  5. Envelope protein requirements for the assembly of infectious virions of porcine reproductive and respiratory syndrome virus. Wissink, E.H., Kroese, M.V., van Wijk, H.A., Rijsewijk, F.A., Meulenberg, J.J., Rottier, P.J. J. Virol. (2005) [Pubmed]
  6. Construction and evaluation of genetically engineered replication-defective porcine reproductive and respiratory syndrome virus vaccine candidates. Welch, S.K., Jolie, R., Pearce, D.S., Koertje, W.D., Fuog, E., Shields, S.L., Yoo, D., Calvert, J.G. Vet. Immunol. Immunopathol. (2004) [Pubmed]
  7. Monoclonal antibodies against conformationally dependent epitopes on porcine reproductive and respiratory syndrome virus. Zhang, Y., Sharma, R.D., Paul, P.S. Vet. Microbiol. (1998) [Pubmed]
 
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