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dc.contributor.authorIyarit Thaipisuttikulen_US
dc.contributor.authorLauren E. Hittleen_US
dc.contributor.authorRamesh Chandraen_US
dc.contributor.authorDaniel Zangarien_US
dc.contributor.authorCharneal L. Dixonen_US
dc.contributor.authorTeresa A. Garretten_US
dc.contributor.authorDavid A. Raskoen_US
dc.contributor.authorNandini Dasguptaen_US
dc.contributor.authorSamuel M. Moskowitzen_US
dc.contributor.authorLars Malmströmen_US
dc.contributor.authorDavid R. Goodletten_US
dc.contributor.authorSamuel I. Milleren_US
dc.contributor.authorRussell E. Bishopen_US
dc.contributor.authorRobert K. Ernsten_US
dc.contributor.otherUniversity of Maryland, Baltimoreen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherMcMaster University, Faculty of Health Sciencesen_US
dc.contributor.otherVassar Collegeen_US
dc.contributor.otherMassachusetts General Hospitalen_US
dc.contributor.otherHarvard Medical Schoolen_US
dc.contributor.otherETH Zurichen_US
dc.contributor.otherUniversity of Maryland School of Pharmacyen_US
dc.contributor.otherUniversity of Washington, Seattleen_US
dc.date.accessioned2018-11-09T02:01:26Z-
dc.date.available2018-11-09T02:01:26Z-
dc.date.issued2014-01-01en_US
dc.identifier.citationMolecular Microbiology. Vol.91, No.1 (2014), 158-174en_US
dc.identifier.issn13652958en_US
dc.identifier.issn0950382Xen_US
dc.identifier.other2-s2.0-84891147285en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84891147285&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/33512-
dc.description.abstractStrains of Pseudomonas aeruginosa (PA) isolated from the airways of cystic fibrosis patients constitutively add palmitate to lipid A, the membrane anchor of lipopolysaccharide. The PhoPQ regulated enzyme PagP is responsible for the transfer of palmitate from outer membrane phospholipids to lipid A. This enzyme had previously been identified in many pathogenic Gram-negative bacteria, but in PA had remained elusive, despite abundant evidence that its lipid A contains palmitate. Using a combined genetic and biochemical approach, we identified PA1343 as the PA gene encoding PagP. Although PA1343 lacks obvious primary structural similarity with known PagP enzymes, the β-barrel tertiary structure with an interior hydrocarbon ruler appears to be conserved. PA PagP transfers palmitate to the 3′ position of lipid A, in contrast to the 2 position seen with the enterobacterial PagP. Palmitoylated PA lipid A alters host innate immune responses, including increased resistance to some antimicrobial peptides and an elevated pro-inflammatory response, consistent with the synthesis of a hexa-acylated structure preferentially recognized by the TLR4/MD2 complex. Palmitoylation commonly confers resistance to cationic antimicrobial peptides, however, increased cytokine production resulting in inflammation is not seen with other palmitoylated lipid A, indicating a unique role for this modification in PA pathogenesis. © 2013 John Wiley & Sons Ltd.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84891147285&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleA divergent Pseudomonas aeruginosa palmitoyltransferase essential for cystic fibrosis-specific lipid Aen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1111/mmi.12451en_US
Appears in Collections:Scopus 2011-2015

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