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dc.contributor.authorBoyd, Aoife
dc.identifier.citationBoyd A, I Lambermont and GR Cornelis. (2000) 'Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: Role of the SycE chaperone binding domain of YopE'. Journal of Bacteriology, 182 :4811-4821.en_US
dc.description.abstractA type III secretion-translocation system allows Yersinia adhering at the surface of animal cells to deliver a cocktail of effector Yops (YopH, -O, -P, -E, -M, and -T) into the cytosol of these cells. Residues or codons 1 to 77 contain all the information required for the complete delivery of YopE into the target cell (release from the bacterium and translocation across the eukaryotic cell membrane). Residues or codons 1 to 15 are sufficient for release from the wild-type bacterium under Ca2+-chelating conditions but not for delivery into target cells. Residues 15 to 50 comprise the binding domain for SycE, a chaperone specific for YopE that is necessary for release and translocation of full-length YopE. To understand the role of this chaperone, we studied the delivery of YopE-Cya reporter proteins and YopE deletants by polymutant Yersinia devoid of most of the Yop effectors ([delta]HOPEM and [delta]THE strains). We first tested YopE-Cya hybrid proteins and YopE proteins deleted of the SycE-binding site. In contrast to wild-type strains, these mutants delivered YopE15-Cya as efficiently as YopE130-Cya. They were also able to deliver YopE [delta]17-77. SycE was dispensable for these deliveries. These results show that residues or codons 1 to 15 are sufficient for delivery into eukaryotic cells and that there is no specific translocation signal in Yops. However, the fact that the SycE-binding site and SycE were necessary for delivery of YopE by wild-type Yersinia suggests that they could introduce hierarchy among the effectors to be delivered. We then tested a YopE-Cya hybrid and YopE proteins deleted of amino acids 2 to 15 but containing the SycE-binding domain. These constructs were neither released in vitro upon Ca2+ chelation nor delivered into cells by wild-type or polymutant bacteria, casting doubts on the hypothesis that SycE could be a secretion pilot. Finally, it appeared that residues 50 to 77 are inhibitory to YopE release and that binding of SycE overcomes this inhibitory effect. Removal of this domain allowed in vitro release and delivery in cells in the absence as well as in the presence of SycE.en_US
dc.description.sponsorshipH. and A. Brenninkmeijer ICP fellowship EU TMR Programme Research Network contract FMRX-CT98-0164 Belgian Fonds National de la Recherche Scientifique Medicale (Convention 3.4595.97) Direction generale de la Recherche Scientifique-Communaute Francaise de Belgique (Action de Recherche Concertee 94/99-172) Interuniversity Poles of Attraction Program-Belgian State, Prime Minister's Office, Federal Office for Scientific, Technical and Cultural affairs (PAI 4/03).en_US
dc.publisherAmerican Society for Microbiologyen_US
dc.relation.ispartofJournal of Bacteriologyen
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Ireland
dc.subjectYersinia enterocoliticaen_US
dc.titleCompetition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: Role of the SycE chaperone binding domain of YopEen_US
dc.local.contactAoife Boyd, Dept. Of Microbiology, Arts/Science Building, Nui Galway. 2404 Email:

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