Identification of genes encoding glycosyltransferases involved in lipopolysaccharide synthesis in Porphyromonas gingivalis.
Mol Oral Microbiol
; 33(1): 68-80, 2018 02.
Article
in En
| MEDLINE
| ID: mdl-28972686
ABSTRACT
Porphyromonas gingivalis can synthesize both A-LPS and O-LPS lipopolysaccharides, which contain anionic O-polysaccharides and conventional O-polysaccharides, respectively. A-LPS can anchor virulence proteins to the cell surface, so elucidating the mechanism of A-LPS synthesis is important for understanding the pathogenicity of this bacterium. To identify the genes involved in LPS synthesis, we focused on uncharacterized genes encoding the glycosyltransferases, PGN_0361, PGN_1239, PGN_1240 and PGN_1668, which were tentatively named gtfC, gtfD, gtfE and gtfF, respectively, and characterized their mutants. We found that disruption of gtfC and gtfF resulted in A-LPS deficiency. In addition, a gtfD mutant had abnormal A-LPS synthesis, and a gtfE mutant exhibited a rough-type LPS that possesses a short oligosaccharide with lipid A-core. We then constructed a gtfC and gtfD double mutant, because their amino acid sequences were very similar, and this mutant similarly possessed a rough-type LPS. Cross-complementation analysis revealed that the GtfD protein is a functional homologue of the Escherichia coli WbbL protein, which is a rhamnosyltransferase. These results suggested that the GtfE protein is essential for the synthesis of both O-LPS and A-LPS, and that GtfC and GtfD proteins may work together to synthesize the two kinds of LPS. In addition, the GtfF protein was essential for A-LPS synthesis, although this may be achieved in a strain-specific manner.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Lipopolysaccharides
/
Glycosyltransferases
/
Porphyromonas gingivalis
/
Genes, Bacterial
Type of study:
Diagnostic_studies
Language:
En
Journal:
Mol Oral Microbiol
Year:
2018
Document type:
Article
Affiliation country:
Japón