Epitope mapping by deletion mutants and chimeras of two vesicular stomatitis virus glycoprotein genes expressed by a vaccinia virus vector

Keil, Walter; Wagner, Robert R.

doi:10.1016/0042-6822(89)90430-3

Cited by 40 publications

(44 citation statements)

References 24 publications

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“…The VSNJV glycoprotein (G NJ ) contains 517 amino acids, and the glycosylation sites are identical to those of G I , but it is not acylated (17). The VSIV and VSNJV glycoproteins also differ in their antigenic structures (24). In general, neutralizing monoclonal antibodies do not cross-react between the G proteins of the two serotypes.…”

mentioning

confidence: 99%

Vesicular Stomatitis Virus Glycoprotein Is a Determinant of Pathogenesis in Swine, a Natural Host

Martı́nez

Rodrı́guez

Jiménez

et al. 2003

J Virol

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There are two major serotypes of vesicular stomatitis virus (VSV), Indiana (VSIV) and New Jersey (VSNJV). We recovered recombinant VSIVs from engineered cDNAs that contained either (i) one copy of the VSIV G gene (VSIV-GI); (ii) two copies of the G gene, one from each serotype (VSIV-GNJGI); or (iii) a single copy of the GNJ gene instead of the GI gene (VSIV-GNJ). The recombinant viruses expressed the appropriate glycoproteins, incorporated them into virions, and were neutralized by antibodies specific for VSIV (VSIV-GI), VSNJV (VSIV-GNJ), or both (VSIV-GNJGI), according to the glycoprotein(s) they expressed. All recombinant viruses grew to similar titers in cell culture. In mice, VSIV-GNJ and VSIV-GNJGI were attenuated. However, in swine, a natural host for VSV, the GNJ glycoprotein-containing viruses caused more severe lesions and replicated to higher titers than the parental virus, VSIV-GI. These observations implicate the glycoprotein as a determinant of VSV virulence in a natural host and emphasize the differences in VSV pathogenesis between mice and swine

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confidence: 99%

Vesicular Stomatitis Virus Glycoprotein Is a Determinant of Pathogenesis in Swine, a Natural Host

Martı́nez

Rodrı́guez

Jiménez

et al. 2003

J Virol

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“…Sequencing of MAb neutralization resistant (MAR) mutants of rabies (Benmansour et al 1991, Raux et al 1995, VSV (Vandepol et al 1986, Luo et al 1988, IHNV (Kim et al 1994) and VHSV (Bearzotti et al 1995) has suggested that 2 regions being distant in the primary structure of the gpG might be associated in the native conformational stage of the protein. Only a few linear reduction-resistant neutralization epitopes have been identified in rabies (VanDeerHeijden et al 1993, Ni et al 1995, VSV (LeFrancois & Lyles 1982, Volk et al 1982, Keil & Wagner 1989, Grigera et al 1992 and IHNV (Leong et al 1995) but none yet in VHSV (Lorenzen et al 1990, Sanz & Col1 1992. The present study focusses on mapping of linear antibody epitopes on the gpG of VHSV.…”

Section: Introductionmentioning

confidence: 99%

“…Reduction of the disulfide bonds of the gpG inhibited the binding of many neutralizing monoclonal antibodies (MAbs) to rhabdoviruses such as rabies (Benmansour et al 1991), vesicular stomatitis virus, VSV (Keil & Wagner 1989), VHSV (Lorenzen et al 1990, Bearzotti et al 1995 and infectious haematopoietic necrosis virus, IHNV (Kim et al 1994, Huang et al 1996. Sequencing of MAb neutralization resistant (MAR) mutants of rabies (Benmansour et al 1991, Raux et al 1995, VSV (Vandepol et al 1986, Luo et al 1988, IHNV (Kim et al 1994) and VHSV (Bearzotti et al 1995) has suggested that 2 regions being distant in the primary structure of the gpG might be associated in the native conformational stage of the protein.…”

Section: Introductionmentioning

confidence: 99%

Mapping of linear antibody epitopes of the glycoprotein of VHSV, a salmonid rhabdovirus

Fernandez‐Alonso¹,

Lorenzo²,

Pérez³

et al. 1998

Dis. Aquat. Org.

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Antibody linear epitopes of the glycoprotein G (gpG) of the viral haemorrhagic septicaemia virus (VHSV), a rhabdovirus of salrnonids, were mapped by pepscan using overlapping 15-mer peptides covering the entire gpG sequence and ELISA with polyclonal and monoclonal murine and polyclonal trout antibodies. Among the regions recognized in the pepscan by the polyclonal antibodies (PAbs) were the previously identified phosphatidylserine binding heptad-repeats (Estepa & Col1 1996; Virology 216:60-70) and leucocyte stimulating peptides (Lorenzo et al. 1995; Virology 212:348-355). Among 17 monoclonal antibodies (MAbs), only 2 non-neutralizing MAbs, 110 (aa 139-153) and IPlH3 (aa 399-413), could b e mapped to specific peptides in the pepscan of the gpG. Mapping of these MAbs was confirmed by immunoblotting with recombinant proteins and/or other synthetic peptides covering those sequences.None of the neutralizing MAbs tested reacted with any of the gpG peptides. Previously mapped MAb resistant mutants in the gpG did not coincide with any of the linear epitopes defined by the pepscan strategy, suggesting the complementarity of the 2 methods for the identification of antibody recogn~tion sites.

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“…Seven of the nine epitopes identified for VSV (NJ) have been mapped to the region of the viral glycoprotein bounded by amino acids 193-289. Included among these seven epitopes were those recognized by the four neutralizing monoclonal antibodies (Keil and Wagner, 1989). Four epitopes including two neutralizing epitopes have been mapped for VSV (Ind) G protein .…”

mentioning

confidence: 99%

“…Four epitopes including two neutralizing epitopes have been mapped for VSV (Ind) G protein . These were located in the cysteine-rich region of amino acids 80-183 near the N-terminus, and another seven epitopes, which also included two neutralizing epitopes, were mapped to a region near the C-terminus between amino acids 286 and 428 (Keil and Wagner, 1989).…”

mentioning

confidence: 99%

Evaluation of a Subunit Vaccine to Infectious Hematopoietic Necrosis Virus, July 31, 1988 to September 20, 1989 Annual Report.

Leong¹

1989

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Epitope mapping by deletion mutants and chimeras of two vesicular stomatitis virus glycoprotein genes expressed by a vaccinia virus vector

Cited by 40 publications

References 24 publications

Vesicular Stomatitis Virus Glycoprotein Is a Determinant of Pathogenesis in Swine, a Natural Host

Vesicular Stomatitis Virus Glycoprotein Is a Determinant of Pathogenesis in Swine, a Natural Host

Mapping of linear antibody epitopes of the glycoprotein of VHSV, a salmonid rhabdovirus

Evaluation of a Subunit Vaccine to Infectious Hematopoietic Necrosis Virus, July 31, 1988 to September 20, 1989 Annual Report.

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