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Gene Review

TCRVsSgp1  -  glycoprotein

Tacaribe virus

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Disease relevance of TCRVsSgp1

  • The envelope glycoprotein of the arenaviruses (GP-C) is unusual in that the mature complex retains the cleaved, 58-amino-acid signal peptide [1].
  • These are completely conserved among the predicted polyprotein sequences of all the CCHF virus strains and closely resemble the tetrapeptides that represent the major cleavage recognition sites present in the glycoprotein precursors of arenaviruses, such as Lassa fever virus (RRLL) and Pichinde virus (RKLL) [2].
  • Having established that the heterologous glycoprotein protects against JUNV challenge, a recombinant vaccinia virus was constructed that expresses JUNV glycoprotein precursor (VV-GJun) [3].
  • Effect of inhibitors of the intracellular exocytic pathway on glycoprotein processing and maturation of Junin virus [4].
  • Drug resistant variants were isolated, suggesting that these compounds act through inhibition of a viral protein, the viral glycoprotein (GP2), and not through cellular toxicity mechanisms [5].

High impact information on TCRVsSgp1


Chemical compound and disease context of TCRVsSgp1

  • The influence of glycoprotein processing, cleavage and transport on Junin virus (JV) infectivity was investigated using monensin combined with lectin binding assays [10].
  • The effect of glycoprotein processing and transport on Junin virus (JV) maturation was studied by using brefeldin A (BFA) and carbonyl cyanide m-chlorophenylhydrazone (CCCP), two inhibitors affecting different steps of the intracellular exocytic pathway, combined with low temperature incubation [4].
  • The biological properties mediated by the main envelope glycoprotein (GP1) of a mouse-attenuated mutant of Junin virus, named Cl67, were investigated in comparison with its parental strain XJCl3 [11].

Anatomical context of TCRVsSgp1

  • The cytoskeleton retained nearly 70% of the external JV envelope glycoprotein GP38 and about 40% of the JV nucleoprotein NP, according to TX-100 and OG insolubility results [12].
  • Neutralizing antibodies against the main viral glycoprotein (GP38) inhibited syncytium production and GP38 conformational changes in response to acid treatment were detected by an immunoprecipitation assay [13].
  • Thus, GP38 production together with glycoprotein transport to the cell membrane seemed to be required for the release of infectious virus from JV-infected cells [10].
  • Thus, results obtained with BFA allow to conclude that the proteolytic processing of GPC probably occurs at the trans-Golgi network and this cleavage together with the glycoprotein presence at the cell surface is required for maturation of infectious JV particles [4].


  1. Role of the stable signal peptide of Junín arenavirus envelope glycoprotein in pH-dependent membrane fusion. York, J., Nunberg, J.H. J. Virol. (2006) [Pubmed]
  2. Characterization of the glycoproteins of Crimean-Congo hemorrhagic fever virus. Sanchez, A.J., Vincent, M.J., Nichol, S.T. J. Virol. (2002) [Pubmed]
  3. Homologous and heterologous glycoproteins induce protection against Junin virus challenge in guinea pigs. López, N., Scolaro, L., Rossi, C., Jácamo, R., Candurra, N., Pujol, C., Damonte, E.B., Franze-Fernández, M.T. J. Gen. Virol. (2000) [Pubmed]
  4. Effect of inhibitors of the intracellular exocytic pathway on glycoprotein processing and maturation of Junin virus. Candurra, N.A., Damonte, E.B. Arch. Virol. (1997) [Pubmed]
  5. Identification and characterization of potent small molecule inhibitor of hemorrhagic fever New World arenaviruses. Bolken, T.C., Laquerre, S., Zhang, Y., Bailey, T.R., Pevear, D.C., Kickner, S.S., Sperzel, L.E., Jones, K.F., Warren, T.K., Amanda Lund, S., Kirkwood-Watts, D.L., King, D.S., Shurtleff, A.C., Guttieri, M.C., Deng, Y., Bleam, M., Hruby, D.E. Antiviral Res. (2006) [Pubmed]
  6. The signal peptide of the Junín arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex. York, J., Romanowski, V., Lu, M., Nunberg, J.H. J. Virol. (2004) [Pubmed]
  7. Tacaribe virus Z protein interacts with the L polymerase protein to inhibit viral RNA synthesis. Jácamo, R., López, N., Wilda, M., Franze-Fernández, M.T. J. Virol. (2003) [Pubmed]
  8. Inhibition of cell fusion in Junin virus-infected cells by sera from Argentine hemorrhagic fever patients. Castilla, V., Contigiani, M., Mersich, S.E. J. Clin. Virol. (2005) [Pubmed]
  9. Analysis of viral glycoproteins by glycosidic digestion inside a polyacrylamide gel. Grutadauria, S., Castilla, V., Zapata, M., Mersich, S. J. Virol. Methods (1999) [Pubmed]
  10. Intracellular processing and transport of Junin virus glycoproteins influences virion infectivity. Damonte, E.B., Mersich, S.E., Candurra, N.A. Virus Res. (1994) [Pubmed]
  11. Glycoprotein-mediated biological properties of a host range mutant of Junin virus. Scolaro, L.A., Damonte, E.B. Res. Virol. (1997) [Pubmed]
  12. Involvement of the cytoskeleton in Junin virus multiplication. Candurra, N.A., Lago, M.J., Maskin, L., Damonte, E.B. J. Gen. Virol. (1999) [Pubmed]
  13. Low-pH-induced fusion of Vero cells infected with Junin virus. Castilla, V., Mersich, S.E. Arch. Virol. (1996) [Pubmed]
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