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Type-specific immunogenicity of a chemically synthesized peptide fragment of type 5 streptococcal M protein

We determined the antigenic specificity and protective immunogenicity of two chemically synthesized peptides of type 5 streptococcal M protein. The synthetic peptides, designated S-M5(1-20) and S-M5(20-40), represent the amino-terminal amino acid sequence of the native pepsin- extracted M5 molecule,...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1983
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187117/
https://www.ncbi.nlm.nih.gov/pubmed/6195292
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collection PubMed
description We determined the antigenic specificity and protective immunogenicity of two chemically synthesized peptides of type 5 streptococcal M protein. The synthetic peptides, designated S-M5(1-20) and S-M5(20-40), represent the amino-terminal amino acid sequence of the native pepsin- extracted M5 molecule, which is known to contain at least one heart cross-reactive epitope. Initial studies showed that neither of the synthetic peptides was able to bind purified heart-reactive M5 antibodies. In addition, S-M5(1-20), but not S-M5(20-40), contained type-specific antigenic determinants as measured by enzyme-linked immunosorbent inhibition assays. When covalently linked to tetanus toxoid, S-M5(1-20), but not S-M5(20-40), evoked significant levels of type-specific, opsonic (and presumably protective) antibodies in rabbits without evoking heart cross-reactive antibodies.
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spelling pubmed-21871172008-04-17 Type-specific immunogenicity of a chemically synthesized peptide fragment of type 5 streptococcal M protein J Exp Med Articles We determined the antigenic specificity and protective immunogenicity of two chemically synthesized peptides of type 5 streptococcal M protein. The synthetic peptides, designated S-M5(1-20) and S-M5(20-40), represent the amino-terminal amino acid sequence of the native pepsin- extracted M5 molecule, which is known to contain at least one heart cross-reactive epitope. Initial studies showed that neither of the synthetic peptides was able to bind purified heart-reactive M5 antibodies. In addition, S-M5(1-20), but not S-M5(20-40), contained type-specific antigenic determinants as measured by enzyme-linked immunosorbent inhibition assays. When covalently linked to tetanus toxoid, S-M5(1-20), but not S-M5(20-40), evoked significant levels of type-specific, opsonic (and presumably protective) antibodies in rabbits without evoking heart cross-reactive antibodies. The Rockefeller University Press 1983-11-01 /pmc/articles/PMC2187117/ /pubmed/6195292 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Type-specific immunogenicity of a chemically synthesized peptide fragment of type 5 streptococcal M protein
title Type-specific immunogenicity of a chemically synthesized peptide fragment of type 5 streptococcal M protein
title_full Type-specific immunogenicity of a chemically synthesized peptide fragment of type 5 streptococcal M protein
title_fullStr Type-specific immunogenicity of a chemically synthesized peptide fragment of type 5 streptococcal M protein
title_full_unstemmed Type-specific immunogenicity of a chemically synthesized peptide fragment of type 5 streptococcal M protein
title_short Type-specific immunogenicity of a chemically synthesized peptide fragment of type 5 streptococcal M protein
title_sort type-specific immunogenicity of a chemically synthesized peptide fragment of type 5 streptococcal m protein
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187117/
https://www.ncbi.nlm.nih.gov/pubmed/6195292