The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species

Eric P. Skaar, Deborah M. Tobiason, J. Quick, Ralph C. Juddt, Herbert Weissbach, Frantzy Etienne, Nathan Brot, H. Steven Seifert*

*Corresponding author for this work

Research output: Contribution to journalArticle

101 Scopus citations

Abstract

The PilB protein of Neisseria gonorrhoeae has been reported to be involved in the regulation of pilin gene transcription, but it also possesses significant homology to the peptide methionine sulfoxide reductase family of enzymes, specifically MsrA and MsrB from Escherichia coli. MsrA and MsrB in E. coli are able to reduce methionine sulfoxide residues in proteins to methionines. In addition, the gonococcal PilB protein encodes for both MsrA and MsrB activity associated with the repair of oxidative damage to proteins. In this work, we demonstrate that the PilB protein of Neisseria gonorrhoeae is not involved in pilus expression. Additionally, we show that wild-type N. gonorrhoeae produces two forms of this polypeptide, one of which contains a signal sequence and is secreted from the bacterial cytoplasm to the outer membrane; the other lacks a signal sequence and is cytoplasmic. Furthermore, we show that the secreted form of the PilB protein is involved in survival in the presence of oxidative damage.

Original languageEnglish (US)
Pages (from-to)10108-10113
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number15
DOIs
StatePublished - Jul 23 2002

ASJC Scopus subject areas

  • General

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