Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Proteomics of Aggregatibacter actinomycetemcomitans Outer Membrane Vesicles
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Medicine, Department of Odontology.
Umeå University, Faculty of Medicine, Department of Odontology.
2015 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 10, no 9, e0138591Article in journal (Refereed) Published
Abstract [en]

Aggregatibacter actinomycetemcomitans is an oral and systemic pathogen associated with aggressive forms of periodontitis and with endocarditis. Outer membrane vesicles (OMVs) released by this species have been demonstrated to deliver effector proteins such as cytolethal distending toxin (CDT) and leukotoxin (LtxA) into human host cells and to act as triggers of innate immunity upon carriage of NOD1- and NOD2-active pathogen-associated molecular patterns (PAMPs). To improve our understanding of the pathogenicity-associated functions that A. actinomycetemcomitans exports via OMVs, we studied the proteome of density gradient-purified OMVs from a rough-colony type clinical isolate, strain 173 (serotype e) using liquid chromatography-tandem mass spectrometry (LC-MS/MS). This analysis yielded the identification of 151 proteins, which were found in at least three out of four independent experiments. Data are available via ProteomeXchange with identifier PXD002509. Through this study, we not only confirmed the vesicle-associated release of LtxA, and the presence of proteins, which are known to act as immunoreactive antigens in the human host, but we also identified numerous additional putative virulence-related proteins in the A. actinomycetemcomitans OMV proteome. The known and putative functions of these proteins include immune evasion, drug targeting, and iron/nutrient acquisition. In summary, our findings are consistent with an OMV-associated proteome that exhibits several offensive and defensive functions, and they provide a comprehensive basis to further disclose roles of A. actinomycetemcomitans OMVs in periodontal and systemic disease.

Place, publisher, year, edition, pages
2015. Vol. 10, no 9, e0138591
National Category
Medical and Health Sciences Clinical Medicine
Identifiers
URN: urn:nbn:se:umu:diva-110086DOI: 10.1371/journal.pone.0138591ISI: 000361790200135PubMedID: 26381655OAI: oai:DiVA.org:umu-110086DiVA: diva2:861112
Available from: 2015-10-15 Created: 2015-10-15 Last updated: 2017-12-01Bibliographically approved

Open Access in DiVA

fulltext(3988 kB)84 downloads
File information
File name FULLTEXT01.pdfFile size 3988 kBChecksum SHA-512
8535d3c0b213917441532948ab8d36e702ed9348d8ee2f57fc8ae2e8c2f0367eee7090165d9fff3daf03b7352baead8e64d1113e26804a4efa1c8b5caf9df3c5
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Kieselbach, ThomasGranström, ElisabethOscarsson, Jan
By organisation
Department of ChemistryDepartment of Odontology
In the same journal
PLoS ONE
Medical and Health SciencesClinical Medicine

Search outside of DiVA

GoogleGoogle Scholar
Total: 84 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 214 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf