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Identification of an O-antigen chain length regulator, WzzP, in Porphyromonas gingivalis


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Title: Identification of an O-antigen chain length regulator, WzzP, in Porphyromonas gingivalis
Authors: Shoji, Mikio / Yukitake, Hideharu / Sato, Keiko / Shibata, Yasuko / Naito, Mariko / Aduse-Opoku, Joseph / Abiko, Yoshimitsu / Curtis, Michael A. / Nakayama, Koji
Issue Date: Jun-2013
Publisher: John Wiley and Sons Inc.
Citation: MicrobiologyOpen, 2(3), pp.383-401; 2013
Abstract: 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.
Keywords: LPS biosynthesis / Periodontal pathogen / WbaP protein / Wzx protein / Wzz protein
URI: http://hdl.handle.net/10069/34411
ISSN: 20458827
DOI: 10.1002/mbo3.84
Rights: © 2013 The Authors. Microbiology Open published by John Wiley & Sons Ltd. / This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Type: Journal Article
Text Version: publisher
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/34411

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