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Domain analysis of lipoprotein LppQ in Mycoplasma mycoides subsp. mycoides SC

Bonvin-Klotz, Laetitia ; Vilei, Edy ; Kühni-Boghenbor, Kathrin ; Kapp, Nadine ; Frey, Joachim ; Stoffel, Michael

In: Antonie van Leeuwenhoek, 2008, vol. 93, no. 1-2, p. 175-183

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    Titre
    • Domain analysis of lipoprotein LppQ in Mycoplasma mycoides subsp. mycoides SC
    Auteur
    • Bonvin-Klotz, Laetitia. Division of Veterinary Anatomy, Vetsuisse Faculty, University of Bern, Postfach, 3001, Bern, Switzerland
    • Vilei, Edy. Institute of Veterinary Bacteriology, Vetsuisse Faculty, University of Bern, Postfach, 3001, Bern, Switzerland
    • Kühni-Boghenbor, Kathrin. Division of Veterinary Anatomy, Vetsuisse Faculty, University of Bern, Postfach, 3001, Bern, Switzerland
    • Kapp, Nadine. Division of Veterinary Anatomy, Vetsuisse Faculty, University of Bern, Postfach, 3001, Bern, Switzerland
    • Frey, Joachim. Institute of Veterinary Bacteriology, Vetsuisse Faculty, University of Bern, Postfach, 3001, Bern, Switzerland
    • Stoffel, Michael. Division of Veterinary Anatomy, Vetsuisse Faculty, University of Bern, Postfach, 3001, Bern, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Antonie van Leeuwenhoek, 2008, vol. 93, no. 1-2, p. 175-183. Springer Netherlands
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:310162
    Summary
    The lipoprotein LppQ is the most prominent antigen of Mycoplasma mycoides subsp. mycoides small colony type (SC) during infection of cattle. This pathogen causes contagious bovine pleuropneumonia (CBPP), a devastating disease of considerable socio-economic importance in many countries worldwide. The dominant antigenicity and high specificity for M. mycoides subsp. mycoides SC of lipoprotein LppQ have been exploited for serological diagnosis and for epidemiological investigations of CBPP. Scanning electron microscopy and immunogold labelling were used to provide ultrastructural evidence that LppQ is located to the cell membrane at the outer surface of M. mycoides subsp. mycoides SC. The selectivity and specificity of this method were demonstrated through discriminating localization of extracellular (i.e., in the zone of contact with host cells) vs. integral membrane domains of LppQ. Thus, our findings support the suggestion that the accessible N-terminal domain of LppQ is surface exposed and such surface localization may be implicated in the pathogenesis of CBPP