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dc.contributor.authorPokrajac, Lisa A.
dc.contributor.authorHarris, J. Robin
dc.contributor.authorSarraf, Naghmeh S
dc.contributor.authorPalmer, Michael
dc.date.accessioned2017-04-13 17:17:44 (GMT)
dc.date.available2017-04-13 17:17:44 (GMT)
dc.date.issued2013-04
dc.identifier.urihttps://doi.org/10.1139/bcb-2012-0065
dc.identifier.urihttp://hdl.handle.net/10012/11660
dc.descriptionFinal version of this article is published by NRC Research Press and available at: http://dx.doi.org/10.1139/bcb-2012-0065en
dc.description.abstractPyolysin (PLO) belongs to the homologous family of the cholesterol-dependent cytolysins (CDCs), which bind to cell membranes containing cholesterol to form oligomeric pores of large size. The CDC monomer structure consists of 4 domains. Among these, the C-terminal domain 4 has been implicated in membrane binding of the monomer, while the subsequent processes of oligomerization and membrane insertion have primarily been assigned to other domains of the molecule. Recombinantly expressed or proteolytic fragments that span domain 4 of the CDCs streptolysin O and perfringolysin O bind to membranes but fail to oligomerize, and they inhibit the activity of the respective wild-type toxins. We report here that the isolated domain 4 of pyolysin (PLO-D4) not only binds to membranes but also forms oligomers with itself, as well as hybrid oligomers with the full-length toxin. As expected, the pure PLO-D4 oligomers are devoid of pore-forming activity. Surprisingly, however, within hybrid oligomers, PLO-D4 not only fails to inhibit, but even amplifies the hemolytic activity of the full-length toxin, to an extent similar to that of doubling the amount of the full-length toxin alone. We propose that this amplification may be related to the kinetics of the oligomerization reaction. Overall, our findings indicate a greater role of domain 4 in the oligomerization of CDCs than previously demonstrated.en
dc.description.sponsorshipThis study was supported by an operating grant from NSERC to M. Palmer.en
dc.language.isoenen
dc.publisherNRC Research Pressen
dc.subjectArcanobacterium actinomyces pyogenesen
dc.subjectCholesterolen
dc.subjectClostridium-perfringensen
dc.subjectFragmenten
dc.subjectHemolysisen
dc.subjectInsertionen
dc.subjectMechanismen
dc.subjectMembrane-bindingen
dc.subjectOligomerizationen
dc.subjectPore formationen
dc.subjectPyolysinen
dc.subjectStreptolysin-oen
dc.subjectTheta-toxinen
dc.subjectThiol-activated cytolysinen
dc.titleOligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysinen
dc.typeArticleen
dcterms.bibliographicCitationPokrajac, L., Harris, J. R., Sarraf, N., & Palmer, M. (2013). Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysin. Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire, 91(2), 59–66. https://doi.org/10.1139/bcb-2012-0065en
uws.contributor.affiliation1Faculty of Scienceen
uws.contributor.affiliation2Chemistryen
uws.typeOfResourceTexten
uws.peerReviewStatusRevieweden
uws.scholarLevelFacultyen


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