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Virulence of Yersinia enterocolitica is closely associated with siderophore production, expression of an iron‐repressible outer membrane polypeptide of 65 000 Da and pesticin sensitivity
Author(s) -
Heesemann Jürgen,
Hantke Klaus,
Vocke Tilman,
Saken Elizabeth,
Rakin Alexander,
Stojiljkovic Igor,
Berner Reinhard
Publication year - 1993
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1993.tb01583.x
Subject(s) - siderophore , yersinia enterocolitica , biology , microbiology and biotechnology , bacterial outer membrane , virulence , yersinia , enterobacteriaceae , yersinia pseudotuberculosis , escherichia coli , serotype , pathogenicity island , bacteria , gene , biochemistry , genetics
Summary Iron‐repressible outer membrane proteins (Irp) and siderophore production of Yersinia enterocolitica , serotype 08, were subjected to analysis. Here four Irps of apparent molecular weights of 62000, 65000, 74000 and 75000 could be identified which were expressed constitutively by a fur mutant. Production of a novel catechol‐containing siderophore (denoted yersiniabactin) was detected by siderophore‐indicator agar (chrome azurol S) and feeding experiments. Growth support by yersiniabactin under iron‐restricted conditions was TonB‐ and Irp65‐dependent and correlated with pesticin‐sensitivity of Yersinia enterocolitica and Escherichia coli ø. From these results we conclude that Irp65 of Y. enterocolitica functions as yersiniabactin receptor (FyuA) and as pesticin receptor. By immunoblotting using rabbit antibodies against Irp65 and chrome azurol S‐agar, we were able to demonstrate that all tested mouse‐lethai Y. enterocoiitica and Yersinia pseudotuberculosis strains of different serotypes express siderophores and Irp65. Moreover, the anti‐lrp65 rabbit serum did not cross‐react with the known iron‐repressible high‐molecular‐weight proteins (HMWPs). Evidently, the mouse lethality trait in enteropathogenic Yersinia spp. is closely associated with a novel iron‐uptake system, comprising the production of a siderophore and a siderophore receptor of apparent molecular mass 65 000 Da.