期刊
MICROBIOLOGYOPEN
卷 2, 期 3, 页码 383-401出版社
WILEY
DOI: 10.1002/mbo3.84
关键词
LPS biosynthesis; periodontal pathogen; WbaP protein; Wzx protein; Wzz protein
类别
资金
- Ministry of Education, Science, Sports, Culture, and Technology, Japan [20249073, 23792110]
- Global COE Program at Nagasaki University
- Nagasaki University, Japan
- Grants-in-Aid for Scientific Research [25293375, 24117006, 25462863, 22592078, 25462925, 20249073, 23792110] Funding Source: KAKEN
The periodontal pathogen Porphyromonas gingivalis has two different lipopolysaccharides (LPSs) designated O-LPS and A-LPS, which are a conventional O-antigen polysaccharide and an anionic polysaccharide that are both linked to lipid A-cores, respectively. However, the precise mechanisms of LPS biosynthesis remain to be determined. In this study, we isolated a pigment-less mutant by transposon mutagenesis and identified that the transposon was inserted into the coding sequence PGN_2005, which encodes a hypothetical protein of P. gingivalis ATCC 33277. We found that (i) LPSs purified from the PGN_2005 mutant were shorter than those of the wild type; (ii) the PGN_2005 protein was located in the inner membrane fraction; and (iii) the PGN_2005 gene conferred Wzz activity upon an Escherichia coli wzz mutant. These results indicate that the PGN_2005 protein, which was designated WzzP, is a functional homolog of the Wzz protein in P. gingivalis. Comparison of amino acid sequences among WzzP and conventional Wzz proteins indicated that WzzP had an additional fragment at the C-terminal region. In addition, we determined that the PGN_1896 and PGN_1233 proteins and the PGN_1033 protein appear to be WbaP homolog proteins and a Wzx homolog protein involved in LPS biosynthesis, respectively.
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