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Gene Review

NS3  -  non structural polyprotein NS3

Palyam virus

 
 
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Disease relevance of NS3

  • However, the RNA encoding NS3 and NS3A, and the two segments encoding the outer capsid proteins, are more variable between the AHSV serotypes [1].
  • Release of bluetongue virus-like particles from insect cells is mediated by BTV nonstructural protein NS3/NS3A [2].
  • Further, we show that the C-terminal domain of NS3 interacts with VP2, the outermost protein of the fully assembled virus particle, suggesting that NS3 forms a bridging molecule that draws assembled virus into contact with the cellular export machinery [3].
  • Spodoptera frugiperda cells infected with the recombinant baculovirus synthesized two polypeptides, which were shown to represent NS3 and NS3A by Western blot (immunoblot) and peptide map analysis [4].
  • The smallest RNA segment (S10) of bluetongue virus (an orbivirus, family Reoviridae) encodes two closely related nonstructural proteins, the 229-amino-acid (aa) NS3 and the 216-aa NS3A [5].
 

High impact information on NS3

  • To test this hypothesis, variation in the consensus sequence and quasispecies heterogeneity of the VP2 and NS3/NS3A genes of a plaque-purified strain of BTV serotype 10 was determined during alternating infection of vector Culicoides sonorensis and a sheep and calf [6].
  • Occurrence of genetic drift and founder effect during quasispecies evolution of the VP2 and NS3/NS3A genes of bluetongue virus upon passage between sheep, cattle, and Culicoides sonorensis [6].
  • Membrane organization of bluetongue virus nonstructural glycoprotein NS3 [5].
  • Our data indicate that both hydrophobic domains of NS3 span the cell membrane and that only the site at aa 150 is responsible for N-linked glycosylation of the NS3 proteins [5].
  • The NS3/NS3A proteins have two hydrophobic domains (aa 118 to 141 and 162 to 182) and two potential asparagine-linked glycosylation sites (aa 63 and 150), one of which is located between the hydrophobic domains [5].
 

Chemical compound and disease context of NS3

  • Adaptation of bluetongue virus (BTV) to grow in mosquito cells (C6/36) resulted in overexpression of two non-structural proteins (NS3 and NS3a) in infected cells [7].
 

Biological context of NS3

  • This report focuses on the nonstructural proteins NS1 and NS3, which are encoded by genome segments 5 and 10 respectively [8].
  • Comparison of the amino acid sequences of NS3 of AHSV-3 and AHSV-9 identified two areas of approximately 45 amino acids which displayed high (98%) similarity [9].
  • Collectively, the data indicate that NS3 and NS3a may be involved in the final stages of BTV morphogenesis, i.e. the release of BTV from infected cells [10].
  • The smallest viral genome segment, S10, encodes two small nonstructural proteins, NS3 and NS3A, which mediate the release of virus particles from infected cells and may subsequently influence the natural dispersion of these viruses [11].
  • The inferred phylogeny of AHSV NS3 corresponded well with the described NS3 phylogenetic clusters [12].
 

Anatomical context of NS3

  • The simultaneous expression of the nonstructural NS1 or NS3/NS3A proteins with CLPs did not lead to the association of such particles with the cytoskeleton, nor to their release from cells [2].
  • In vitro translation of bluetongue virus (BTV) double-stranded RNA in the rabbit reticulocyte lysate system has shown segment 10 (S10) to code for two related proteins, NS3 and NS3A [4].
  • In the presence of cycloheximide, NS3 and NS3A immunofluorescence staining was pronounced in the Golgi complex, confirming that NS3 and NS3A are competent for transport to the Golgi apparatus after synthesis [13].
  • Studies on AHSV-3 infected Vero cells showed that equimolar amounts of NS3 and NS3A were synthesized [14].
 

Associations of NS3 with chemical compounds

  • Conserved features in all AHSV NS3 proteins include the synthesis of a truncated NS3A protein from the same open reading frame as that of NS3, a proline-rich region, a region of strict sequence conservation and two hydrophobic domains [15].
 

Other interactions of NS3

  • In addition to the seven structural proteins that are coded by seven of the RNA species, four non-structural proteins, NS1, NS2, NS3 and NS3A, are coded by three RNA segments, M5, S8 and S10 [1].
  • Genome segments 5 and 10 encode the smaller outer capsid protein VP5 and the non structural proteins NS3/NS3a, respectively [16].
 

Analytical, diagnostic and therapeutic context of NS3

  • The sensitivity of the EHDV PCR assay was increased by chemiluminescent hybridization; by this EHDV-NS3 PCR, 10 fg of EHDV RNA was detected (equivalent to 600 viral particles) [17].
  • Each of the S10 genes encoded two proteins NS3 and NS3A, which were shown to be related by peptide mapping [9].
  • 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 [18].

References

  1. African horse sickness virus structure. Roy, P., Mertens, P.P., Casal, I. Comp. Immunol. Microbiol. Infect. Dis. (1994) [Pubmed]
  2. Release of bluetongue virus-like particles from insect cells is mediated by BTV nonstructural protein NS3/NS3A. Hyatt, A.D., Zhao, Y., Roy, P. Virology (1993) [Pubmed]
  3. The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release. Beaton, A.R., Rodriguez, J., Reddy, Y.K., Roy, P. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  4. Expression of two related nonstructural proteins of bluetongue virus (BTV) type 10 in insect cells by a recombinant baculovirus: production of polyclonal ascitic fluid and characterization of the gene product in BTV-infected BHK cells. French, T.J., Inumaru, S., Roy, P. J. Virol. (1989) [Pubmed]
  5. Membrane organization of bluetongue virus nonstructural glycoprotein NS3. Bansal, O.B., Stokes, A., Bansal, A., Bishop, D., Roy, P. J. Virol. (1998) [Pubmed]
  6. Occurrence of genetic drift and founder effect during quasispecies evolution of the VP2 and NS3/NS3A genes of bluetongue virus upon passage between sheep, cattle, and Culicoides sonorensis. Bonneau, K.R., Mullens, B.A., MacLachlan, N.J. J. Virol. (2001) [Pubmed]
  7. Adaptation of bluetongue virus in mosquito cells results in overexpression of NS3 proteins and release of virus particles. Guirakhoo, F., Catalan, J.A., Monath, T.P. Arch. Virol. (1995) [Pubmed]
  8. Characterization of two African horse sickness virus nonstructural proteins, NS1 and NS3. van Staden, V., Smit, C.C., Stoltz, M.A., Maree, F.F., Huismans, H. Arch. Virol. Suppl. (1998) [Pubmed]
  9. A comparison of the genes which encode non-structural protein NS3 of different orbiviruses. van Staden, V., Huismans, H. J. Gen. Virol. (1991) [Pubmed]
  10. Localization of the non-structural protein NS3 in bluetongue virus-infected cells. Hyatt, A.D., Gould, A.R., Coupar, B., Eaton, B.T. J. Gen. Virol. (1991) [Pubmed]
  11. Variation in the NS3 gene and protein in South African isolates of bluetongue and equine encephalosis viruses. van Niekerk, M., Freeman, M., Paweska, J.T., Howell, P.G., Guthrie, A.J., Potgieter, A.C., van Staden, V., Huismans, H. J. Gen. Virol. (2003) [Pubmed]
  12. Variation of African horsesickness virus nonstructural protein NS3 in southern Africa. van Niekerk , M., van Staden , V., van Dijk , A.A., Huismans, H. J. Gen. Virol. (2001) [Pubmed]
  13. Multiple glycoproteins synthesized by the smallest RNA segment (S10) of bluetongue virus. Wu, X., Chen, S.Y., Iwata, H., Compans, R.W., Roy, P. J. Virol. (1992) [Pubmed]
  14. Expression of nonstructural protein NS3 of African horsesickness virus (AHSV): evidence for a cytotoxic effect of NS3 in insect cells, and characterization of the gene products in AHSV infected Vero cells. van Staden, V., Stoltz, M.A., Huismans, H. Arch. Virol. (1995) [Pubmed]
  15. Membrane association of African horsesickness virus nonstructural protein NS3 determines its cytotoxicity. van Niekerk, M., Smit, C.C., Fick, W.C., van Staden, V., Huismans, H. Virology (2001) [Pubmed]
  16. Development of a mouse model system, coding assignments and identification of the genome segments controlling virulence of African horse sickness virus serotypes 3 and 8. O'Hara, R.S., Meyer, A.J., Burroughs, J.N., Pullen, L., Martin, L.A., Mertens, P.P. Arch. Virol. Suppl. (1998) [Pubmed]
  17. PCR detection of North American and Central African isolates of epizootic hemorrhagic disease virus (EHDV) based on genome segment 10 of EHDV serotype 1. Aradaib, I.E., Wilson, W.C., Schore, C.E., Mohammed, M.E., Yilma, T.D., Cullor, J.S., Osburn, B.I. J. Clin. Microbiol. (1998) [Pubmed]
  18. 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]
 
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