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A surface receptor specific for human IgA on group B streptococci possessing the Ibc protein antigen

A number of group B streptococcal strains of various serotypes, Ia, Ib, Ic, II, and III were examined for their ability to bind human IgG and IgA. No strains of group B streptococci were found to bind IgG, but many strains possessing the Ibc protein antigen(s) were found to bind a significant amount...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1984
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187502/
https://www.ncbi.nlm.nih.gov/pubmed/6387034
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description A number of group B streptococcal strains of various serotypes, Ia, Ib, Ic, II, and III were examined for their ability to bind human IgG and IgA. No strains of group B streptococci were found to bind IgG, but many strains possessing the Ibc protein antigen(s) were found to bind a significant amount of IgA. The extent of IgA binding correlated with the amount of a 130,000 mol wt, detergent-extractable protein, and reactivity with the Ic typing sera. Using nitrocellulose blots, it was found that the 130,000 mol wt protein bound human IgA. A method was developed to purify the protein while retaining its ability to bind human IgA. Using solid phase radioimmunoassays, it was determined that the protein bound to the Fc region of monomeric or polymeric IgA and that it failed to bind IgM or any IgG isotype.
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spelling pubmed-21875022008-04-17 A surface receptor specific for human IgA on group B streptococci possessing the Ibc protein antigen J Exp Med Articles A number of group B streptococcal strains of various serotypes, Ia, Ib, Ic, II, and III were examined for their ability to bind human IgG and IgA. No strains of group B streptococci were found to bind IgG, but many strains possessing the Ibc protein antigen(s) were found to bind a significant amount of IgA. The extent of IgA binding correlated with the amount of a 130,000 mol wt, detergent-extractable protein, and reactivity with the Ic typing sera. Using nitrocellulose blots, it was found that the 130,000 mol wt protein bound human IgA. A method was developed to purify the protein while retaining its ability to bind human IgA. Using solid phase radioimmunoassays, it was determined that the protein bound to the Fc region of monomeric or polymeric IgA and that it failed to bind IgM or any IgG isotype. The Rockefeller University Press 1984-11-01 /pmc/articles/PMC2187502/ /pubmed/6387034 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
A surface receptor specific for human IgA on group B streptococci possessing the Ibc protein antigen
title A surface receptor specific for human IgA on group B streptococci possessing the Ibc protein antigen
title_full A surface receptor specific for human IgA on group B streptococci possessing the Ibc protein antigen
title_fullStr A surface receptor specific for human IgA on group B streptococci possessing the Ibc protein antigen
title_full_unstemmed A surface receptor specific for human IgA on group B streptococci possessing the Ibc protein antigen
title_short A surface receptor specific for human IgA on group B streptococci possessing the Ibc protein antigen
title_sort surface receptor specific for human iga on group b streptococci possessing the ibc protein antigen
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187502/
https://www.ncbi.nlm.nih.gov/pubmed/6387034