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Recombinant Porphyromonas gingivalis FimA preproprotein expressed in Escherichia coli is lipidated and the mature or processed recombinant FimA protein forms a short filament in vitro.


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Title: Recombinant Porphyromonas gingivalis FimA preproprotein expressed in Escherichia coli is lipidated and the mature or processed recombinant FimA protein forms a short filament in vitro.
Authors: Shoji, Mikio / Yoshimura, Atsutoshi / Yoshioka, Hidenobu / Takade, Akemi / Takuma, Yasuko / Yukitake, Hideharu / Naito, Mariko / Hara, Yoshitaka / Yoshida, Shin-Ichi / Nakayama, Koji
Issue Date: Nov-2010
Publisher: Canadian Science Publishing
Citation: Canadian Journal of Microbiology, 56(11), pp.959-967; 2010
Abstract: The gram-negative anaerobic bacterium Porphyromonas gingivalis is an etiologically important pathogen for chronic periodontal diseases in adults. Our previous study suggested that the major structural components of both Fim and Mfa fimbriae in this organism are secreted through their lipidated precursors. In this study, we constructed Escherichia coli strains expressing various fimA genes with or without the 5'-terminal DNA region encoding the signal peptide, and we determined whether lipidation of recombinant FimA proteins occurred in E. coli. Lipidation occurred for a recombinant protein from the fimA gene with the 5'-terminal DNA region encoding the signal peptide but not for a recombinant protein from the fimA gene without the signal-peptide-encoding region, as revealed by [3H]palmitic acid labeling experiments. A TLR2-dependent signaling response was induced by the recombinant protein from the fimA gene with the signal-peptide-encoding region but not by a recombinant protein from the fimA gene with the signal-peptide-encoding region that had a base substitution causing an amino acid substitution (C19A). Electron microscopic analysis revealed that recombinant FimA (A-47 - W-383) protein was autopolymerized to form filamentous structures of about 80 nm in length in vitro. The results suggest that FimA protein, a major subunit of Fim fimbriae, is transported to the outer membrane by the lipoprotein sorting system, and a mature or processed FimA protein on the outer membrane is autopolymerized to form Fim fimbriae.
Description: This is a revised document of the article published in Canadian Journal of Microbiology, 56(11), pp.959-967; 2010. The contents of modification is published in Canadian Journal of Microbiology, 57(1), pp.68; 2011. It is available at http://dx.doi.org/10.1139/W10-114.
Keywords: Fimbriae / Lipoprotein / Porphyromonas gingivalis / Recombinant FimA protein / TLR2
URI: http://hdl.handle.net/10069/25139
ISSN: 00084166
DOI: 10.1139/w10-084
PubMed ID: 21076487
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/25139

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