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Moraxella catarrhalis expresses a cardiolipin synthase that impacts adherence to human epithelial cells.
- Source :
-
Journal of bacteriology [J Bacteriol] 2014 Jan; Vol. 196 (1), pp. 107-20. Date of Electronic Publication: 2013 Oct 18. - Publication Year :
- 2014
-
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.
- Subjects :
- Cell Line
DNA Mutational Analysis
DNA, Bacterial chemistry
DNA, Bacterial genetics
Escherichia coli Proteins genetics
Gene Deletion
Hepatocytes microbiology
Humans
Membrane Proteins genetics
Molecular Sequence Data
Moraxella catarrhalis genetics
Mutagenesis, Site-Directed
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Transferases (Other Substituted Phosphate Groups) genetics
Bacterial Adhesion
Cardiolipins biosynthesis
Epithelial Cells microbiology
Membrane Proteins biosynthesis
Moraxella catarrhalis enzymology
Moraxella catarrhalis physiology
Transferases (Other Substituted Phosphate Groups) biosynthesis
Subjects
Details
- Language :
- English
- ISSN :
- 1098-5530
- Volume :
- 196
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of bacteriology
- Publication Type :
- Academic Journal
- Accession number :
- 24142255
- Full Text :
- https://doi.org/10.1128/JB.00298-13