Secretion of Yop proteins by Yersiniae

T Michiels, P Wattiau, R Brasseur, J M Ruysschaert, G Cornelis

    Résultats de recherche: Contribution à un journal/une revueArticleRevue par des pairs


    Upon incubation at 37 degrees C in the absence of Ca2+ ions, pathogenic strains of the genus Yersinia cease growing and produce large amounts of a series of plasmid-encoded proteins involved in pathogenicity. These proteins, called Yops (for Yersinia outer membrane proteins), are detected in both the outer membrane fraction and the culture supernatant. We present here the nucleotide sequence of genes yop20 and yop25 from Yersinia enterocolitica O:9. Protein Yop25 is very similar to YopE, the corresponding protein from Yersinia pestis, Y. pseudotuberculosis, and Y. enterocolitica O:8 (A. Forsberg and H. Wolf-Watz, J. Bacteriol. 172:1547-1555, 1990). This is the first report of a yop20 sequence of yersiniae. We present evidences that Yops are not membrane proteins. Their detection in the membrane fraction results either from copurification of large aggregates of extracellular Yops with the membrane fraction or from the adsorption of released proteins to the cell surface. In contrast with Yops, protein P1 has characteristics of a true membrane protein. The release of Yops by Y. enterocolitica occurs by a novel secretion mechanism that does not involve the cleavage of a typical signal sequence or the recognition of a carboxy-terminal domain.
    langue originaleAnglais
    Pages (de - à)2840-9
    Nombre de pages10
    journalInfection and Immunity
    Numéro de publication9
    Etat de la publicationPublié - 1990

    Empreinte digitale

    Examiner les sujets de recherche de « Secretion of Yop proteins by Yersiniae ». Ensemble, ils forment une empreinte digitale unique.

    Contient cette citation