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AN OUTER MEMBRANE PROTEIN OF NEISSERIA MENINGITIDIS GROUP B RESPONSIBLE FOR SEROTYPE SPECIFICITY

Meningococcal groups B and C have been subdivided into a series of serotypes based upon the antigenic specificity of protein serotype antigens (STA). The purpose of these studies was to obtain the STA by gentle methods and determine its anatomic location in the meningococcal cell. The STA was extrac...

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Detalles Bibliográficos
Autores principales: Frasch, Carl E., Gotschlich, Emil C.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1974
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139694/
https://www.ncbi.nlm.nih.gov/pubmed/4134571
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author Frasch, Carl E.
Gotschlich, Emil C.
author_facet Frasch, Carl E.
Gotschlich, Emil C.
author_sort Frasch, Carl E.
collection PubMed
description Meningococcal groups B and C have been subdivided into a series of serotypes based upon the antigenic specificity of protein serotype antigens (STA). The purpose of these studies was to obtain the STA by gentle methods and determine its anatomic location in the meningococcal cell. The STA was extracted from group B meningococcal strains by either 0.2 M LiCl or 0.2 M CaCl(2) and isolated from the extracts by gel filtration on Sepharose 6B or by pelleting the STA by centrifugation at 100,000 g. The isolated STA was a lipoprotein-lipopolysaccharide complex with a mol wt of approximately 4 x 10(6) daltons. Antisera prepared against the type 2 STA were bactericidal only for homologous serotype strains. The STA proved to be a constituent of the outer membrane of the cell envelope. This was shown by SDS-polyacrylamide gel electrophoresis (PAGE) of the isolated outer membrane and of the purified STA. The type 2 STA complex contains three principal proteins, one of which is predominant with a mol wt of 41,000 daltons. The type 2 STA was dissociated by Triton X-100 and separated by sucrose gradient isodensity centrifugation into two peaks. The denser peak (ρ = 1.26 g/cm(3)) contained the majority of the 41,000 dalton major outer membrane protein as shown by SDS-PAGE. This peak also contained the type 2 antigenic determinant. Thus the major outer membrane protein, extracted as part of a lipoprotein-lipopolysaccharide complex, contains the type 2 STA determinant.
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spelling pubmed-21396942008-04-17 AN OUTER MEMBRANE PROTEIN OF NEISSERIA MENINGITIDIS GROUP B RESPONSIBLE FOR SEROTYPE SPECIFICITY Frasch, Carl E. Gotschlich, Emil C. J Exp Med Article Meningococcal groups B and C have been subdivided into a series of serotypes based upon the antigenic specificity of protein serotype antigens (STA). The purpose of these studies was to obtain the STA by gentle methods and determine its anatomic location in the meningococcal cell. The STA was extracted from group B meningococcal strains by either 0.2 M LiCl or 0.2 M CaCl(2) and isolated from the extracts by gel filtration on Sepharose 6B or by pelleting the STA by centrifugation at 100,000 g. The isolated STA was a lipoprotein-lipopolysaccharide complex with a mol wt of approximately 4 x 10(6) daltons. Antisera prepared against the type 2 STA were bactericidal only for homologous serotype strains. The STA proved to be a constituent of the outer membrane of the cell envelope. This was shown by SDS-polyacrylamide gel electrophoresis (PAGE) of the isolated outer membrane and of the purified STA. The type 2 STA complex contains three principal proteins, one of which is predominant with a mol wt of 41,000 daltons. The type 2 STA was dissociated by Triton X-100 and separated by sucrose gradient isodensity centrifugation into two peaks. The denser peak (ρ = 1.26 g/cm(3)) contained the majority of the 41,000 dalton major outer membrane protein as shown by SDS-PAGE. This peak also contained the type 2 antigenic determinant. Thus the major outer membrane protein, extracted as part of a lipoprotein-lipopolysaccharide complex, contains the type 2 STA determinant. The Rockefeller University Press 1974-07-01 /pmc/articles/PMC2139694/ /pubmed/4134571 Text en Copyright © 1974 by The Rockefeller University Press 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 Article
Frasch, Carl E.
Gotschlich, Emil C.
AN OUTER MEMBRANE PROTEIN OF NEISSERIA MENINGITIDIS GROUP B RESPONSIBLE FOR SEROTYPE SPECIFICITY
title AN OUTER MEMBRANE PROTEIN OF NEISSERIA MENINGITIDIS GROUP B RESPONSIBLE FOR SEROTYPE SPECIFICITY
title_full AN OUTER MEMBRANE PROTEIN OF NEISSERIA MENINGITIDIS GROUP B RESPONSIBLE FOR SEROTYPE SPECIFICITY
title_fullStr AN OUTER MEMBRANE PROTEIN OF NEISSERIA MENINGITIDIS GROUP B RESPONSIBLE FOR SEROTYPE SPECIFICITY
title_full_unstemmed AN OUTER MEMBRANE PROTEIN OF NEISSERIA MENINGITIDIS GROUP B RESPONSIBLE FOR SEROTYPE SPECIFICITY
title_short AN OUTER MEMBRANE PROTEIN OF NEISSERIA MENINGITIDIS GROUP B RESPONSIBLE FOR SEROTYPE SPECIFICITY
title_sort outer membrane protein of neisseria meningitidis group b responsible for serotype specificity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139694/
https://www.ncbi.nlm.nih.gov/pubmed/4134571
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