Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/2960
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dc.contributor.authorLata, K.-
dc.contributor.authorChattopadhyay, K.-
dc.date.accessioned2020-12-10T07:16:32Z-
dc.date.available2020-12-10T07:16:32Z-
dc.date.issued2014-
dc.identifier.citationBiochemistry,53(22), pp.3553-3563.en_US
dc.identifier.otherhttps://doi.org/10.1021/bi500152n-
dc.identifier.urihttps://pubs.acs.org/doi/10.1021/bi500152n-
dc.identifier.urihttp://hdl.handle.net/123456789/2960-
dc.description.abstractHelicobacter pylori TlyA is a pore-forming hemolysin with potent cytotoxic activity. To explore the potential membrane-damaging activity of H. pylori TlyA, we have studied its interaction with the synthetic liposome vesicles. In our study, H. pylori TlyA shows a prominent ability to associate with the liposome vesicles without displaying an obligatory requirement for any protein receptor on the liposome membranes. Interaction of TlyA triggers agglutination of the liposome vesicles. Such agglutinating activity of TlyA could also be observed with erythrocytes before the induction of its pore-forming hemolytic activity. In addition to its agglutinating activity against liposomes, TlyA also induces fusion and disruption of the liposome membranes. Altogether, our study highlights novel membrane-damaging properties of H. pylori TlyA that have not been documented previously with any other TlyA family protein.en_US
dc.language.isoenen_US
dc.publisherAmerican Chemical Societyen_US
dc.subjectVesiclesen_US
dc.subjectLipidsen_US
dc.subjectFluorescenceen_US
dc.subjectMembranesen_US
dc.subjectAssaysen_US
dc.titleHelicobacter pylori TlyA Agglutinates Liposomes and Induces Fusion and Permeabilization of the Liposome Membranesen_US
dc.typeArticleen_US
Appears in Collections:Research Articles

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