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• W2011908054 abstract "The major phospholipid constituents of Moraxella catarrhalis membranes are phosphatidylglycerol, phosphatidylethanolamine, and cardiolipin (CL). However, very little is known regarding the synthesis and function of these phospholipids in M. catarrhalis. In this study, we discovered that M. catarrhalis expresses a cardiolipin synthase (CLS), termed MclS, that is responsible for the synthesis of CL within the bacterium. The nucleotide sequence of mclS is highly conserved among M. catarrhalis isolates and is predicted to encode a protein with significant amino acid similarity to the recently characterized YmdC/ClsC protein of Escherichia coli. Isogenic mclS mutant strains were generated in M. catarrhalis isolates O35E, O12E, and McGHS1 and contained no observable levels of CL. Site-directed mutagenesis of a highly conserved HKD motif of MclS also resulted in a CL-deficient strain. Moraxella catarrhalis, which depends on adherence to epithelial cells for colonization of the human host, displays significantly reduced levels of adherence to HEp-2 and A549 cell lines in the mclS mutant strains compared to wild-type bacteria. The reduction in adherence appears to be attributed to the absence of CL. These findings mark the first instance in which a CLS has been related to a virulence-associated trait." @default.
• W2011908054 created "2016-06-24" @default.
• W2011908054 creator A5053872371 @default.
• W2011908054 creator A5061954021 @default.
• W2011908054 date "2013-10-18" @default.
• W2011908054 modified "2023-09-25" @default.
• W2011908054 title "Moraxella catarrhalis Expresses a Cardiolipin Synthase That Impacts Adherence to Human Epithelial Cells" @default.
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• W2011908054 doi "https://doi.org/10.1128/jb.00298-13" @default.
• W2011908054 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3911130" @default.
• W2011908054 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24142255" @default.
• W2011908054 hasPublicationYear "2013" @default.
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