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N-propionylated group B meningococcal polysaccharide mimics a unique epitope on group B Neisseria meningitidis
Antibodies induced in mice by the N-propionyl (N-Pr)-group B meningococcal polysaccharide (GBMP)-tetanus toxoid (TT) conjugate were bactericidal for GBM organisms independent of protein serotype. The antisera contained two populations of N-Pr-GBMP-specific antibodies, only one of which crossreacted...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1987
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188568/ https://www.ncbi.nlm.nih.gov/pubmed/2435835 |
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collection | PubMed |
description | Antibodies induced in mice by the N-propionyl (N-Pr)-group B meningococcal polysaccharide (GBMP)-tetanus toxoid (TT) conjugate were bactericidal for GBM organisms independent of protein serotype. The antisera contained two populations of N-Pr-GBMP-specific antibodies, only one of which crossreacted with the GBMP. Particularly significant was the fact that the bactericidal activity was mainly associated with the population of antibodies that did not crossreact with the GBMP. Therefore it can be inferred from the above evidence that the N-Pr-GBMP mimics a unique epitope on the surface of GBM organisms that is not present on the exogenous GBMP. |
format | Text |
id | pubmed-2188568 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1987 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21885682008-04-17 N-propionylated group B meningococcal polysaccharide mimics a unique epitope on group B Neisseria meningitidis J Exp Med Articles Antibodies induced in mice by the N-propionyl (N-Pr)-group B meningococcal polysaccharide (GBMP)-tetanus toxoid (TT) conjugate were bactericidal for GBM organisms independent of protein serotype. The antisera contained two populations of N-Pr-GBMP-specific antibodies, only one of which crossreacted with the GBMP. Particularly significant was the fact that the bactericidal activity was mainly associated with the population of antibodies that did not crossreact with the GBMP. Therefore it can be inferred from the above evidence that the N-Pr-GBMP mimics a unique epitope on the surface of GBM organisms that is not present on the exogenous GBMP. The Rockefeller University Press 1987-04-01 /pmc/articles/PMC2188568/ /pubmed/2435835 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 N-propionylated group B meningococcal polysaccharide mimics a unique epitope on group B Neisseria meningitidis |
title | N-propionylated group B meningococcal polysaccharide mimics a unique epitope on group B Neisseria meningitidis |
title_full | N-propionylated group B meningococcal polysaccharide mimics a unique epitope on group B Neisseria meningitidis |
title_fullStr | N-propionylated group B meningococcal polysaccharide mimics a unique epitope on group B Neisseria meningitidis |
title_full_unstemmed | N-propionylated group B meningococcal polysaccharide mimics a unique epitope on group B Neisseria meningitidis |
title_short | N-propionylated group B meningococcal polysaccharide mimics a unique epitope on group B Neisseria meningitidis |
title_sort | n-propionylated group b meningococcal polysaccharide mimics a unique epitope on group b neisseria meningitidis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188568/ https://www.ncbi.nlm.nih.gov/pubmed/2435835 |