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  • Hasegawa, Y. (author)

Role of Mfa5 in Expression of Mfa1 Fimbriae in Porphyromonas gingivalis

  • Article/chapterEnglish2016

Publisher, publication year, extent ...

  • 2016-07-21
  • International & American Associations for Dental Research,2016
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:umu-124436
  • https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-124436URI
  • https://doi.org/10.1177/0022034516655083DOI

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  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Fimbriae are protein-based filamentous appendages that protrude from the bacterial cell surface and facilitate host adhesion. Two types of fimbriae, FimA and Mfa1, of the periodontal pathogen Porphyromonas gingivalis are responsible for adherence to other bacteria and to host cells in the oral cavity. Both fimbrial forms are composed of 5 proteins, but there is limited information about their polymerization mechanisms. Here, the authors evaluated the function of Mfa5, one of the Mfa1 fimbrial accessory proteins. Using mfa5 gene disruption and complementation studies, the authors revealed that Mfa5 affects the incorporation of other accessory proteins, Mfa3 and Mfa4, into fibers and the expression of fimbriae on the cell surface. Mfa5 is predicted to have a C-terminal domain (CTD) that uses the type IX secretion system (T9SS), which is limited to this organism and related Bacteroidetes species, for translocation across the outer membrane. To determine the relationship between the putative Mfa5 CTD and the T9SS, mutants were constructed with in-frame deletion of the CTD and deletion of porU, a C-terminal signal peptidase linked to T9SS-mediated secretion. The ∆CTD-expressing strain presented a similar phenotype to the mfa5 disruption mutant with reduced expression of fimbriae lacking all accessory proteins. The ∆porU mutants and the ∆CTD-expressing strain showed intracellular accumulation of Mfa5. These results indicate that Mfa5 function requires T9SS-mediated translocation across the outer membrane, which is dependent on the CTD, and subsequent incorporation into fibers. These findings suggest the presence of a novel polymerization mechanism of the P. gingivalis fimbriae.

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  • Iijima, Y. (author)
  • Persson, KarinaUmeå universitet,Kemiska institutionen(Swepub:umu)kape0001 (author)
  • Nagano, K. (author)
  • Yoshida, Y. (author)
  • Lamont, RJ. (author)
  • Kikuchi, T. (author)
  • Mitani, A. (author)
  • Yoshimura, F. (author)
  • Umeå universitetKemiska institutionen (creator_code:org_t)

Related titles

  • In:Journal of Dental Research: International & American Associations for Dental Research95:11, s. 1291-12970022-03451544-0591

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Hasegawa, Y.
Iijima, Y.
Persson, Karina
Nagano, K.
Yoshida, Y.
Lamont, RJ.
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Kikuchi, T.
Mitani, A.
Yoshimura, F.
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About the subject
NATURAL SCIENCES
NATURAL SCIENCES
and Chemical Science ...
NATURAL SCIENCES
NATURAL SCIENCES
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Journal of Denta ...
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Umeå University

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