Simple jQuery Dropdowns
Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/11461
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSunsiree Muangmanen_US
dc.contributor.authorSunee Korbsrisateen_US
dc.contributor.authorVeerachat Muangsombuten_US
dc.contributor.authorVarintip Srinonen_US
dc.contributor.authorNatalie Lazar Adleren_US
dc.contributor.authorGunnar N. Schroederen_US
dc.contributor.authorGad Frankelen_US
dc.contributor.authorEdouard E. Galyoven_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherUniversity of Leicesteren_US
dc.contributor.otherImperial College Londonen_US
dc.date.accessioned2018-05-03T08:00:06Z-
dc.date.available2018-05-03T08:00:06Z-
dc.date.issued2011-10-01en_US
dc.identifier.citationFEMS Microbiology Letters. Vol.323, No.1 (2011), 75-82en_US
dc.identifier.issn15746968en_US
dc.identifier.issn03781097en_US
dc.identifier.other2-s2.0-80052709747en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=80052709747&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/11461-
dc.description.abstractBurkholderia pseudomallei, the causative agent of melioidosis, exploits the Bsa type III secretion system (T3SS) to deliver effector proteins into host cells. These effectors manipulate host cell functions; thus, contributing to the ability of the bacteria to evade the immune response and cause disease. Only two Bsa-secreted effectors have been conclusively identified to date. Here, we report the identification of the third B. pseudomallei type III secreted effector protein, designated BopC. BopC is encoded by the bpss1516 gene abutting bpss1517, which encodes its putative chaperone. The genes are located in the close proximity to the bsa T3SS gene cluster of B. pseudomallei K96243 (Fig. 1). BopC was secreted into culture supernatant by the wild-type B. pseudomallei strain, but its secretion was abolished in the bsaZ T3SS mutant. Using pull down and co-purification assays, we confirmed that BopC interacts with its putative chaperone, BPSS1517, in vitro. Furthermore, the first 20 N-terminal amino acids of BopC were found to be sufficient to mediate the T3SS-dependent translocation of a reporter protein from a heterologous enteropathogenic Escherichia coli host into mammalian cells. Finally, bopC mutant was found to be less invasive than the wild-type strain in the epithelial cells. © 2011 Federation of European Microbiological Societies.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=80052709747&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleBopC is a type III secreted effector protein of Burkholderia pseudomalleien_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1111/j.1574-6968.2011.02359.xen_US
Appears in Collections:Scopus 2011-2015

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.