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

AHSVs7gp1  -  VP7 protein

African horse sickness 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 AHSVs7gp1

  • Comparison of the AHSV-4 VP7 sequence with that of bluetongue virus serotype 10 revealed an overall similarity of 44%, with the amino- and carboxy-terminal regions exhibiting the greatest levels of homology [1].
  • VP7, of African horsesickness virus serotype 4 (AHSV-4) was determined from cDNA analyses and found to be 1179 nucleotides in length [1].
  • Seven site-specific substitution mutations of VP7 have been created using cDNA clones and were employed to produce seven recombinant baculoviruses [2].
  • Functional dissection of the major structural protein of bluetongue virus: identification of key residues within VP7 essential for capsid assembly [2].
  • Either 20 mg of virus particles, 20 mg of ISVPs or 10 mg of cores as well as 20 mg of VP7 crystals could be purified from approximately 8 x 10(9) infected cells [3].
 

High impact information on AHSVs7gp1

 

Chemical compound and disease context of AHSVs7gp1

 

Biological context of AHSVs7gp1

  • Full-length cDNA of the RNA genome segment coding for the major core protein VP7 of Australian bluetongue virus serotype 15 (BTV-15) has been isolated by reverse transcription-PCR cloning [10].
  • Each segment is 1156 bp long and contains an open reading frame encoding the 349-amino acid VP7 protein [11].
  • The nucleotide sequence of segment S1 and the deduced amino acid sequence of VP7 from bluetongue virus (BTV) serotype 13 was determined [12].
  • Because the inner core proteins are involved with infectivity of insect cells, we hypothesized that certain VP7 protein sequences are preferred by the insect vector species present in specific geographic locations [13].
  • The major core protein VP7 and a non-structural protein NS3 of bluetongue virus serotype 1 have been synthesized from recombinant plasmids using both an in vitro transcription/translation system and a yeast expression system [14].
 

Anatomical context of AHSVs7gp1

  • Examination of VP7 in the cytosol of cells infected with either BTV or a vaccinia virus recombinant expressing VP7 indicated that the protein may exist as an oligomer, whose constituent monomers are not linked by intermolecular disulfide bonds [15].
  • Intracellularly, VP7 antibodies also reacted with virus-like particles which appeared to be leaving virus inclusion bodies (VIB), the presumed site of virus synthesis and assembly [16].
  • In Western overalay analysis, the Culicoides plasma membrane preparation reduced binding of an anti-VP7 monoclonal antibody to VP7 [17].
  • With the VP7-specific MAbs a rapid and sensitive double antibody sandwich immunoassay has been developed to detect viral antigen in infected Vero cells and in spleen tissue from AHSV-infected horses [18].
  • Detection of African horsesickness virus in infected spleens by a sandwich ELISA using two monoclonal antibodies specific for VP7 [19].
 

Associations of AHSVs7gp1 with chemical compounds

  • Sequencing of VP7 revealed it to be an extremely hydrophobic protein, 350 amino acids in length with cysteine residues at positions 15, 65, and 154 [15].
  • Denaturation of VP7 with SDS did not eliminate the capacity of the protein to bind MAb 20E9 [15].
  • Most (greater than 94%) of the amino acids of VP7 among the serotypes are conserved, including the location (position 255) of a single lysine residue [11].
  • Analysis of the fluorescent peptides generated by V8 protease cleavage of VP7 labeled with AEDANS in the absence of DTT (i.e., with any putative intramolecular disulfide bonds intact) suggested that the cysteine at position 154 was the only one accessible to AEDANS [15].
  • The size of the labeled peptides and knowledge of the location of potential V8 cleavage sites suggested that the enzyme cleaved VP7 at three locations (glutamic acid residues at positions 61, 104 (or 108), and 132 (or 134 or 135) [15].
 

Analytical, diagnostic and therapeutic context of AHSVs7gp1

  • The structure of AHSV VP7 reveals that during crystallization, the two-domain protein is cleaved and only the top domain remains [8].
  • Interaction of EGFP-VP3 and VP7 and subsequent assembly of core-like particles was further examined by visualizing fluorescent particles and was confirmed by biochemical analysis and by electron microscopy [20].
  • Twelve monoclonal antibodies (MAbs) was generated using purified VP7 or CLPs as a source of antigen and were utilized for epitope mapping with available chimeric VP7 molecules and the RGD mutants [7].
  • Immunoelectron microscopy has been used to confirm that the core protein VP7 is accessible on the surface of bluetongue virus (BTV) particles [15].
  • Bluetongue virus evolution: sequence analyses of the genomic S1 segments and major core protein VP7 [11].

References

  1. The complete sequence of the group-specific antigen, VP7, of African horsesickness disease virus serotype 4 reveals a close relationship to bluetongue virus. Roy, P., Hirasawa, T., Fernandez, M., Blinov, V.M., Sanchez-Vixcain Rodrique, J.M. J. Gen. Virol. (1991) [Pubmed]
  2. Functional dissection of the major structural protein of bluetongue virus: identification of key residues within VP7 essential for capsid assembly. Limn, C.K., Staeuber, N., Monastyrskaya, K., Gouet, P., Roy, P. J. Virol. (2000) [Pubmed]
  3. Purification and properties of virus particles, infectious subviral particles, cores and VP7 crystals of African horsesickness virus serotype 9. Burroughs, J.N., O'Hara, R.S., Smale, C.J., Hamblin, C., Walton, A., Armstrong, R., Mertens, P.P. J. Gen. Virol. (1994) [Pubmed]
  4. Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion. Mathieu, M., Petitpas, I., Navaza, J., Lepault, J., Kohli, E., Pothier, P., Prasad, B.V., Cohen, J., Rey, F.A. EMBO J. (2001) [Pubmed]
  5. The complete nucleotide and deduced amino acid sequence of the gene encoding the major inner capsid protein, VP7 of US bluetongue virus serotype 17. Kowalik, T.F., Li, J.K., Chuang, R.Y., Doi, R.H., Osburn, B.I. Nucleic Acids Res. (1990) [Pubmed]
  6. Sindbis virus vectors designed to express a foreign protein as a cleavable component of the viral structural polyprotein. Thomas, J.M., Klimstra, W.B., Ryman, K.D., Heidner, H.W. J. Virol. (2003) [Pubmed]
  7. RGD tripeptide of bluetongue virus VP7 protein is responsible for core attachment to Culicoides cells. Tan, B.H., Nason, E., Staeuber, N., Jiang, W., Monastryrskaya, K., Roy, P. J. Virol. (2001) [Pubmed]
  8. Crystal structure of the top domain of African horse sickness virus VP7: comparisons with bluetongue virus VP7. Basak, A.K., Gouet, P., Grimes, J., Roy, P., Stuart, D. J. Virol. (1996) [Pubmed]
  9. Induction of antibodies to the bluetongue virus core polypeptide VP7 in sheep by internal image rabbit antiidiotypic antibodies. Lin, M., Zhou, E.M., Heckert, R.A. Viral Immunol. (1996) [Pubmed]
  10. Major core protein VP7 of Australian bluetongue virus serotype 15: sequence and antigenicity divergence from other BTV serotypes. Wang, L.F., Kattenbelt, J.A., Gould, A.R., Pritchard, L.I., Crameri, G.S., Eaton, B.T. J. Gen. Virol. (1994) [Pubmed]
  11. Bluetongue virus evolution: sequence analyses of the genomic S1 segments and major core protein VP7. Kowalik, T.F., Li, J.K. Virology (1991) [Pubmed]
  12. Sequence analyses and structural predictions of double-stranded RNA segment S1 and VP7 from United States prototype bluetongue virus serotypes 13 and 10. Kowalik, T.F., Li, J.K. Virology (1989) [Pubmed]
  13. Phylogenetic relationships of bluetongue viruses based on gene S7. Wilson, W.C., Ma, H.C., Venter, E.H., van Djik, A.A., Seal, B.S., Mecham, J.O. Virus Res. (2000) [Pubmed]
  14. High level expression of the major core protein VP7 and the non-structural protein NS3 of bluetongue virus in yeast: use of expressed VP7 as a diagnostic, group-reactive antigen in a blocking ELISA. Martyn, J.C., Gould, A.R., Eaton, B.T. Virus Res. (1991) [Pubmed]
  15. A bluetongue serogroup-reactive epitope in the amino terminal half of the major core protein VP7 is accessible on the surface of bluetongue virus particles. Eaton, B.T., Gould, A.R., Hyatt, A.D., Coupar, B.E., Martyn, J.C., White, J.R. Virology (1991) [Pubmed]
  16. Ultrastructural distribution of the major capsid proteins within bluetongue virus and infected cells. Hyatt, A.D., Eaton, B.T. J. Gen. Virol. (1988) [Pubmed]
  17. VP7: an attachment protein of bluetongue virus for cellular receptors in Culicoides variipennis. Xu, G., Wilson, W., Mecham, J., Murphy, K., Zhou, E.M., Tabachnick, W. J. Gen. Virol. (1997) [Pubmed]
  18. Diagnostic methods for African horsesickness virus using monoclonal antibodies to structural and non-structural proteins. Ranz, A.I., Miguet, J.G., Anaya, C., Venteo, A., Cortés, E., Vela, C., Sanz, A. Vet. Microbiol. (1992) [Pubmed]
  19. Detection of African horsesickness virus in infected spleens by a sandwich ELISA using two monoclonal antibodies specific for VP7. Laviada, M.D., Babín, M., Dominguez, J., Sánchez-Vizcaíno, J.M. J. Virol. Methods (1992) [Pubmed]
  20. Assembly and intracellular localization of the bluetongue virus core protein VP3. Kar, A.K., Iwatani, N., Roy, P. J. Virol. (2005) [Pubmed]
 
WikiGenes - Universities