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
Helicobacter pylori outer membrane vesicles and the host-pathogen interaction
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
2013 (English)Doctoral thesis, comprehensive summary (Other academic)Alternative title
Helicobacter pylori membranvesiklar och interaktioner med värdcellen (Swedish)
Place, publisher, year, edition, pages
Umeå: Umeå universitet , 2013. , 56 p.
Series
Umeå University medical dissertations, ISSN 0346-6612 ; 1559
Keyword [en]
H. pylori, outer membrane vesicles, 2D 31P, 1H COSY NMR, phospholipids, OMV proteome, adherence, endocytosis, CagA, OMV-host cell responses
Keyword [sv]
yttermembran vesiklar
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:umu:diva-68744ISBN: 978-91-7459-578-9 (print)OAI: oai:DiVA.org:umu-68744DiVA: diva2:617926
Public defence
2013-05-17, KB3B1, KBC-huset, Umeå universitet, Umeå, 09:00 (English)
Opponent
Supervisors
Available from: 2013-04-26 Created: 2013-04-24 Last updated: 2015-11-17Bibliographically approved
List of papers
1. Biochemical and functional characterization of Helicobacter pylori vesicles
Open this publication in new window or tab >>Biochemical and functional characterization of Helicobacter pylori vesicles
Show others...
2010 (English)In: Molecular Microbiology, ISSN 0950-382X, E-ISSN 1365-2958, Vol. 77, no 6, 1539-1555 p.Article in journal (Refereed) Published
Abstract [en]

Helicobacter pylori can cause peptic ulcer disease and/or gastric cancer. Adhesion of bacteria to the stomach mucosa is an important contributor to the vigor of infection and resulting virulence. H. pylori adheres primarily via binding of BabA adhesins to ABO/Lewis b (Leb) blood group antigens and the binding of SabA adhesins to sialyl-Lewis x/a (sLex/a) antigens. Similar to most Gram-negative bacteria, H. pylori continuously buds off vesicles and vesicles derived from pathogenic bacteria often include virulence-associated factors. Here we biochemically characterized highly purified H. pylori vesicles. Major protein and phospholipid components associated with the vesicles were identified with mass spectroscopy and NMR. A subset of virulence factors present was confirmed by immunoblots. Additional functional and biochemical analysis focused on the vesicle BabA and SabA adhesins and their respective interactions to human gastric epithelium. Vesicles exhibit heterogeneity in their protein composition, which were specifically studied in respect to the BabA adhesin. We also demonstrate that the oncoprotein, CagA, is associated with the surface of H. pylori vesicles. Thus, we have explored mechanisms for intimate H. pylori vesicle-host interactions and found that the vesicles carry effector-promoting properties that are important to disease development.

Place, publisher, year, edition, pages
Wiley, 2010
Identifiers
urn:nbn:se:umu:diva-35586 (URN)10.1111/j.1365-2958.2010.07307.x (DOI)000281831400018 ()20659286 (PubMedID)
Available from: 2010-08-24 Created: 2010-08-24 Last updated: 2013-04-26Bibliographically approved
2. Semiconstant-Time P,H-COSY NMR: Analysis of Complex Mixtures of Phospholipids Originating from Helicobacter pylori
Open this publication in new window or tab >>Semiconstant-Time P,H-COSY NMR: Analysis of Complex Mixtures of Phospholipids Originating from Helicobacter pylori
Show others...
2009 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 131, no 40, 14150-1 p.Article in journal (Refereed) Published
Abstract [en]

Lipids play a central role in numerous biological events, ranging from normal physiological processes to host−pathogen interactions. The proposed semiconstant-time 31P,1H−COSY NMR experiment provides identification of known and structural characterization of unknown phospholipids in complex membrane extracts with high sensitivity, based on the combination of their 1H and 31P chemical shifts and coupling patterns. Furthermore, the spectra allow quantification of phospholipid composition. Analysis of the phospholipid composition of Helicobacter pylori, the causative agent of peptic ulcer disease, showed the presence of uncommon phospholipids. This novel NMR approach allows the study of changes in membrane composition in response to biological stimuli and opens up the possibility of identifying soluble phosphorus species in a number of research fields.

Place, publisher, year, edition, pages
ACS Publications ASAP, 2009
Identifiers
urn:nbn:se:umu:diva-26035 (URN)10.1021/ja905282h (DOI)
Note
Publication Date (Web): September 17, 2009Available from: 2009-09-21 Created: 2009-09-21 Last updated: 2013-04-26Bibliographically approved
3. Endocytosis of Helicobacter pylori vesicles
Open this publication in new window or tab >>Endocytosis of Helicobacter pylori vesicles
Show others...
(English)Manuscript (preprint) (Other academic)
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:umu:diva-68749 (URN)
Available from: 2013-04-25 Created: 2013-04-25 Last updated: 2017-05-24
4. Helicobacter pylori vesicles and host cell responses
Open this publication in new window or tab >>Helicobacter pylori vesicles and host cell responses
Show others...
(English)Manuscript (preprint) (Other academic)
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:umu:diva-68750 (URN)
Available from: 2013-04-25 Created: 2013-04-25 Last updated: 2013-04-26

Open Access in DiVA

spikblad(95 kB)33 downloads
File information
File name SPIKBLAD01.pdfFile size 95 kBChecksum SHA-512
496e5b017fda5ed1c580c6b8f1a346bfc43b8a84497da3eb7009cad40221f4b7082a9cabe5f0faac8eb4d24d3e56ce3cebc7b704bb7db1cd00db7bb79b1d9c50
Type spikbladMimetype application/pdf
omslag(2274 kB)6 downloads
File information
File name COVER01.pdfFile size 2274 kBChecksum SHA-512
421efbf87ce76c9dc4179a272c2dbbb4e5c61d1e15127637590b1aaaadb8acfdd5c44bc58f74182dd21f033b4a93212217831ab228d79a6634a4ed3dc6686a47
Type coverMimetype application/pdf
Kappa(2630 kB)236 downloads
File information
File name FULLTEXT01.pdfFile size 2630 kBChecksum SHA-512
cab22529e5ca2c9554a7901435d0e4a99761cd518b614aa77e38b65d393d8cb0b58d6eb50c8ecaece10adaa51586b1186d20bf967379889d552a3e672fc781d4
Type fulltextMimetype application/pdf

Authority records BETA

Olofsson, Annelie

Search in DiVA

By author/editor
Olofsson, Annelie
By organisation
Department of Medical Biochemistry and Biophysics
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

Search outside of DiVA

GoogleGoogle Scholar
Total: 236 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

isbn
urn-nbn

Altmetric score

isbn
urn-nbn
Total: 998 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