PMID: 7540044May 29, 1995Paper

Comparison of the effects of amino acid substitutions and beta-N- vs. alpha-O-glycosylation on the T-cell stimulatory activity and conformation of an epitope on the rabies virus glycoprotein

Biochimica Et Biophysica Acta
L OtvosH C Ertl

Abstract

The first potential N-glycosylation site of the rabies virus glycoprotein, the antigen that carries epitopes for glycoprotein-specific T-cells and virus neutralizing antibodies, is glycosylated inefficiently. Recently, we showed that addition of a beta-N-acetyl-glucosamine moiety to the asparagine residue in the corresponding synthetic fragment V V E D E G C T N L S G F (amino acids 29-41), significantly diminished the T-cell stimulatory activity and reduced the characteristic alpha-helicity of the peptide. The amino acid sequence of the glycoprotein in this region exhibits some degree of variability among different rabies virus and rabies virus related strains, including the replacement of the asparagine residue with aspartic acid or threonine. In the current study, stimulation of a specific T-cell clone by various viral strains and appropriate tridecapeptide sequences and their analogs was investigated. The T-cell recognition pattern of the rabies and rabies-related viruses was identical to that of the synthetic peptides representing the respective epitope sequences. While the asparagine could be replaced without complete loss of T-cell stimulatory activity, amino acid modifications at the C-terminus of the peptide were not t...Continue Reading

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Citations

Apr 25, 2000·Biochemical and Biophysical Research Communications·B TangV P Kurup
Jun 1, 2001·Journal of Immunological Methods·D W KowalczykH C Ertl
Mar 3, 2004·The Journal of Experimental Medicine·Yanfei XuAlessandra Franco
Jul 22, 2005·Immunology and Cell Biology·Yanfei XuAlessandra Franco
Nov 13, 2012·Vaccine·Sergio Rosales-MendozaEdda Sciutto
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Oct 1, 1996·Chemistry & Biology·S E O'Connor, B Imperiali

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