Simple jQuery Dropdowns
Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/42403
Full metadata record
DC FieldValueLanguage
dc.contributor.authorNiramol Jitprasutwiten_US
dc.contributor.authorNurhamimah Zainal-Abidinen_US
dc.contributor.authorCharles Vander Broeken_US
dc.contributor.authorDominic Kurianen_US
dc.contributor.authorSunee Korbsrisateen_US
dc.contributor.authorMark P. Stevensen_US
dc.contributor.authorJoanne M. Stevensen_US
dc.contributor.otherUniversity of Edinburgh, Roslin Instituteen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-12-11T02:05:47Z
dc.date.accessioned2019-03-14T08:03:27Z-
dc.date.available2018-12-11T02:05:47Z
dc.date.available2019-03-14T08:03:27Z-
dc.date.issued2016-12-02en_US
dc.identifier.citationJournal of Proteome Research. Vol.15, No.12 (2016), 4675-4685en_US
dc.identifier.issn15353907en_US
dc.identifier.issn15353893en_US
dc.identifier.other2-s2.0-85000869992en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85000869992&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/42403-
dc.description.abstract© 2016 American Chemical Society. Intracellular actin-based motility of the melioidosis pathogen Burkholderia pseudomallei requires the bacterial factor BimA. Located at one pole of the bacterium, BimA recruits and polymerizes cellular actin to promote bacterial motility within and between cells. Here, we describe an affinity approach coupled with mass spectrometry to identify cellular proteins recruited to BimA-expressing bacteria under conditions that promote actin polymerization. We identified a group of cellular proteins that are recruited to the B. pseudomallei surface in a BimA-dependent manner, a subset of which were independently validated with specific antisera including the ubiquitous scaffold protein Ras GTPase-activating-like protein (IQGAP1). IQGAP1 integrates several key cellular signaling pathways including those involved in actin dynamics and has been shown to be involved in the adhesion of attaching and effacing Escherichia coli to infected cells and invasion of host cells by Salmonella enterica serovar Typhimurium. Although a direct interaction between BimA and IQGAP1 could not be detected using either conventional pulldown or yeast two hybrid techniques, confocal microscopy revealed that IQGAP1 is recruited to B. pseudomallei actin tails in infected cells, and siRNA-mediated knockdown highlighted a role for this protein in controlling the length and actin density of B. pseudomallei actin tails.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85000869992&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemistryen_US
dc.titleIdentification of Candidate Host Cell Factors Required for Actin-Based Motility of Burkholderia pseudomalleien_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1021/acs.jproteome.6b00760en_US
Appears in Collections:Scopus 2016-2017

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.