Fimbriae‐mediated outer membrane vesicle production and invasion of Porphyromonas gingivalis. Issue 1 (18th December 2014)
- Record Type:
- Journal Article
- Title:
- Fimbriae‐mediated outer membrane vesicle production and invasion of Porphyromonas gingivalis. Issue 1 (18th December 2014)
- Main Title:
- Fimbriae‐mediated outer membrane vesicle production and invasion of Porphyromonas gingivalis
- Authors:
- Mantri, Chinmay K.
Chen, Chin‐Ho
Dong, Xinhong
Goodwin, Jeffery Shawn
Pratap, Siddharth
Paromov, Victor
Xie, Hua - Abstract:
- <abstract abstract-type="main" id="mbo3221-abs-0001"> <title>Abstract</title> <p> <italic>Porphyromonas gingivalis</italic> is a keystone periopathogen that plays an essential role in the progress of periodontitis. Like other gram‐negative bacteria, the ability of <italic>P. gingivalis</italic> to produce outer membrane vesicles is a strategy used to interact with, and survive within its biological niches. Here we compared the protein components associated with vesicles derived from a fimbriated strain (33277) and an afimbriated strain (W83) of <italic>P. gingivalis</italic> using proteomic analyses. Some well‐known virulence factors were identified in vesicles from both strains, such as gingipains and hemagglutinin. In contrast, FimC, FimD, and FimE, minor components of long fimbriae were found exclusively in 33277 vesicles, while proteins with a tetratricopeptide repeat (TPR) domain were unique to W83 vesicles. We found that significantly more 33277 than W83 vesicles were internalized into human oral keratinocytes and gingival fibroblasts. Interestingly, FimA, a well‐known adhesin responsible for the attachment and invasion of <italic>P. gingivalis</italic> into host cells, was not essential for the invasive capabilities of <italic>P. gingivalis</italic> vesicles. Rather minor components of long fimbriae were required for an efficient invasive activity of vesicles. The most striking finding was that <italic>P. gingivalis</italic> strains lacking or having a reduced FimA<abstract abstract-type="main" id="mbo3221-abs-0001"> <title>Abstract</title> <p> <italic>Porphyromonas gingivalis</italic> is a keystone periopathogen that plays an essential role in the progress of periodontitis. Like other gram‐negative bacteria, the ability of <italic>P. gingivalis</italic> to produce outer membrane vesicles is a strategy used to interact with, and survive within its biological niches. Here we compared the protein components associated with vesicles derived from a fimbriated strain (33277) and an afimbriated strain (W83) of <italic>P. gingivalis</italic> using proteomic analyses. Some well‐known virulence factors were identified in vesicles from both strains, such as gingipains and hemagglutinin. In contrast, FimC, FimD, and FimE, minor components of long fimbriae were found exclusively in 33277 vesicles, while proteins with a tetratricopeptide repeat (TPR) domain were unique to W83 vesicles. We found that significantly more 33277 than W83 vesicles were internalized into human oral keratinocytes and gingival fibroblasts. Interestingly, FimA, a well‐known adhesin responsible for the attachment and invasion of <italic>P. gingivalis</italic> into host cells, was not essential for the invasive capabilities of <italic>P. gingivalis</italic> vesicles. Rather minor components of long fimbriae were required for an efficient invasive activity of vesicles. The most striking finding was that <italic>P. gingivalis</italic> strains lacking or having a reduced FimA expression showed a significant reduction in vesiculation. These results suggest that production and pathogenicity of <italic>P. gingivalis</italic> vesicles may largely depend on expression of the <italic>fim</italic> locus, and that the integration of vesicle production and pathogenicity with fimbrial expression may allow <italic>P. gingivalis</italic> to confer upon itself certain functional advantages.</p> </abstract> … (more)
- Is Part Of:
- MicrobiologyOpen. Volume 4:Issue 1(2015:Feb.)
- Journal:
- MicrobiologyOpen
- Issue:
- Volume 4:Issue 1(2015:Feb.)
- Issue Display:
- Volume 4, Issue 1 (2015)
- Year:
- 2015
- Volume:
- 4
- Issue:
- 1
- Issue Sort Value:
- 2015-0004-0001-0000
- Page Start:
- 53
- Page End:
- 65
- Publication Date:
- 2014-12-18
- Subjects:
- Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)2045-8827 ↗ - DOI:
- 10.1002/mbo3.221 ↗
- Languages:
- English
- ISSNs:
- 2045-8827
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3347.xml