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. 1992 Mar;60(3):798–803. doi: 10.1128/iai.60.3.798-803.1992

Conserved outer membrane protein of Neisseria meningitidis involved in capsule expression.

M Frosch 1, D Müller 1, K Bousset 1, A Müller 1
PMCID: PMC257557  PMID: 1371768

Abstract

In Neisseria meningitidis, translocation of capsular polysaccharides to the cell surface is mediated by a transport system that fits the characteristics of ABC (ATP-binding cassette) transporters. One protein of this transport system, termed CtrA, is located in the outer membrane. By use of a CtrA-specific monoclonal antibody, we could demonstrate that CtrA occurs exclusively in N. meningitidis and not in other pathogenic or nonpathogenic Neisseria species. Nucleotide sequence comparison of the ctrA gene from different meningococcal serogroups indicated that CtrA is strongly conserved in all meningococcal serogroups, independent of the chemical composition of the capsular polysaccharide. Secondary structure analysis revealed that CtrA is anchored in the outer membrane by eight membrane-spanning amphipathic beta strands, a structure of proteins that function as porins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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