title: Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens.
abstract: Pathogenic bacteria rely on adhesins to bind to host tissues. Therefore, the maintenance of the functional properties of these extracellular macromolecules is essential for the pathogenicity of these microorganisms. We report that peptide methionine sulfoxide reductase (MsrA), a repair enzyme, contributes to the maintenance of adhesins in Streptococcus pneumoniae, Neisseria gonorrhoeae, and Escherichia coli. A screen of a library of pneumococcal mutants for loss of adherence uncovered a MsrA mutant with 75% reduced binding to GalNAcbeta1-4Gal containing eukaryotic cell receptors that are present on type II lung cells and vascular endothelial cells. Subsequently, it was shown that an E. coli msrA mutant displayed decreased type I fimbriae-mediated, mannose-dependent, agglutination of erythrocytes. Previous work [Taha, M. K., So, M., Seifert, H. S., Billyard, E. & Marchal, C. (1988) EMBO J. 7, 4367-4378] has shown that mutants with defects in the pilA-pilB locus from N. gonorrhoeae were altered in their production of type IV pili. We show that pneumococcal MsrA and gonococcal PilB expressed in E. coli have MsrA activity. Together these data suggest that MsrA is required for the proper expression or maintenance of functional adhesins on the surfaces of these three major pathogenic bacteria.
authors: Laboratory of Molecular Infectious Diseases, The Rockefeller University, NY 10021, USA.
authors: T M
authors: TM
authors: Wizemann
authors: J
authors: J
authors: Moskovitz
authors: B J
authors: BJ
authors: Pearce
authors: D
authors: D
authors: Cundell
authors: C G
authors: CG
authors: Arvidson
authors: M
authors: M
authors: So
authors: H
authors: H
authors: Weissbach
authors: N
authors: N
authors: Brot
authors: H R
authors: HR
authors: Masure
mesh_terms: D018829:Adhesins, Bacterial / Q000096:biosynthesis*; D000595:Amino Acid Sequence; D000818:Animals; D001422:Bacterial Adhesion / Q000235:genetics / Q000502:physiology*; D001483:Base Sequence; D002240:Carbohydrate Sequence; D017931:DNA Primers; D004187:Disaccharides / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity; D015870:Gene Expression; D006001:Glycoconjugates; D006168:Guinea Pigs; D006386:Hemagglutination Tests; D051150:Methionine Sulfoxide Reductases; D008969:Molecular Sequence Data; D009344:Neisseria gonorrhoeae / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity; D010088:Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism*; D010980:Platelet Membrane Glycoproteins / Q000502:physiology; D016133:Polymerase Chain Reaction; D011956:Receptors, Cell Surface; D043562:Receptors, G-Protein-Coupled; D017386:Sequence Homology, Amino Acid; D013296:Streptococcus pneumoniae / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity
chemical_list: D018829:Adhesins, Bacterial; D017931:DNA Primers; D004187:Disaccharides; D006001:Glycoconjugates; D010980:Platelet Membrane Glycoproteins; D011956:Receptors, Cell Surface; D043562:Receptors, G-Protein-Coupled; C039351:platelet activating factor receptor; D010088:Oxidoreductases; D051150:Methionine Sulfoxide Reductases; C027219:methionine sulfoxide reductase