@article{oai:nagasaki-u.repo.nii.ac.jp:00005347,
 author = {Shoji, Mikio and Yukitake, Hideharu and Sato, Keiko and Shibata, Yasuko and Naito, Mariko and Aduse-Opoku, Joseph and Abiko, Yoshimitsu and Curtis, Michael A. and Nakayama, Koji},
 issue = {3},
 journal = {MicrobiologyOpen},
 month = {Jun},
 note = {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., MicrobiologyOpen, 2(3), pp.383-401; 2013},
 pages = {383--401},
 title = {Identification of an O-antigen chain length regulator, WzzP, in Porphyromonas gingivalis},
 volume = {2},
 year = {2013}
}