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Host discrimination of Mycoplasma pneumoniae proteinaceous immunogens

The immune response of experimentally infected hamsters and human patients to Mycoplasma pneumoniae was examined by radioimmunoprecipation in conjunction with gel electrophoresis and fluorography. Both intrinsically and extrinsically labeled mycoplasma proteins were coincubated with acute and conval...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1983
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2186949/
https://www.ncbi.nlm.nih.gov/pubmed/6401796
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description The immune response of experimentally infected hamsters and human patients to Mycoplasma pneumoniae was examined by radioimmunoprecipation in conjunction with gel electrophoresis and fluorography. Both intrinsically and extrinsically labeled mycoplasma proteins were coincubated with acute and convalescent sera in a radioimmunoprecipitation assay. Two M. pneumoniae proteins were selectively precipitated by convalescent sera. These predominant immunogens were trypsin-sensitive, antibody-accessible surface proteins that co-migrate on polyacrylamide gels with proteins P1 and P2, which were previously implicated by us as mediators of cytadsorption. Anti-M. pneumoniae antiserum did not precipitate radiolabeled antigens derived from Mycoplasma orale or Mycoplasma salivarium. These data indicate that M. pneumoniae infection stimulates a specific and highly targeted host antibody response to key proteinaceous immunogens.
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spelling pubmed-21869492008-04-17 Host discrimination of Mycoplasma pneumoniae proteinaceous immunogens J Exp Med Articles The immune response of experimentally infected hamsters and human patients to Mycoplasma pneumoniae was examined by radioimmunoprecipation in conjunction with gel electrophoresis and fluorography. Both intrinsically and extrinsically labeled mycoplasma proteins were coincubated with acute and convalescent sera in a radioimmunoprecipitation assay. Two M. pneumoniae proteins were selectively precipitated by convalescent sera. These predominant immunogens were trypsin-sensitive, antibody-accessible surface proteins that co-migrate on polyacrylamide gels with proteins P1 and P2, which were previously implicated by us as mediators of cytadsorption. Anti-M. pneumoniae antiserum did not precipitate radiolabeled antigens derived from Mycoplasma orale or Mycoplasma salivarium. These data indicate that M. pneumoniae infection stimulates a specific and highly targeted host antibody response to key proteinaceous immunogens. The Rockefeller University Press 1983-02-01 /pmc/articles/PMC2186949/ /pubmed/6401796 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
Host discrimination of Mycoplasma pneumoniae proteinaceous immunogens
title Host discrimination of Mycoplasma pneumoniae proteinaceous immunogens
title_full Host discrimination of Mycoplasma pneumoniae proteinaceous immunogens
title_fullStr Host discrimination of Mycoplasma pneumoniae proteinaceous immunogens
title_full_unstemmed Host discrimination of Mycoplasma pneumoniae proteinaceous immunogens
title_short Host discrimination of Mycoplasma pneumoniae proteinaceous immunogens
title_sort host discrimination of mycoplasma pneumoniae proteinaceous immunogens
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2186949/
https://www.ncbi.nlm.nih.gov/pubmed/6401796