title: The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species.
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.
authors.affiliation: Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, 303 East Chicago Avenue, Searle 6-497, Chicago, IL 60611, USA.
authors.forename: Eric P
authors.initials: EP
authors.lastname: Skaar
authors.forename: Deborah M
authors.initials: DM
authors.lastname: Tobiason
authors.forename: J
authors.initials: J
authors.lastname: Quick
authors.forename: Ralph C
authors.initials: RC
authors.lastname: Judd
authors.forename: Herbert
authors.initials: H
authors.lastname: Weissbach
authors.forename: Frantzy
authors.initials: F
authors.lastname: Etienne
authors.forename: Nathan
authors.initials: N
authors.lastname: Brot
authors.forename: H Steven
authors.initials: HS
authors.lastname: Seifert
mesh_terms: D000469:Alkaline Phosphatase / Q000032:analysis; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology*; D017931:DNA Primers; D010861:Fimbriae, Bacterial / Q000502:physiology / Q000648:ultrastructure; D006861:Hydrogen Peroxide / Q000494:pharmacology; D026901:Membrane Transport Proteins; D051150:Methionine Sulfoxide Reductases; D016296:Mutagenesis; D016254:Mutagenesis, Insertional; D009344:Neisseria gonorrhoeae / Q000166:cytology / Q000187:drug effects / Q000235:genetics / Q000502:physiology*; D010088:Oxidoreductases / Q000235:genetics / Q000502:physiology*; D017382:Reactive Oxygen Species / Q000378:metabolism*; D020133:Reverse Transcriptase Polymerase Chain Reaction
chemical_list: D001426:Bacterial Proteins; D017931:DNA Primers; D026901:Membrane Transport Proteins; D017382:Reactive Oxygen Species; C066202:msrA protein, Staphylococcus epidermidis; D006861:Hydrogen Peroxide; D010088:Oxidoreductases; D051150:Methionine Sulfoxide Reductases; C027219:methionine sulfoxide reductase; D000469:Alkaline Phosphatase