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Expression and localization of α- and β-carbonic anhydrase in Helicobacter pylori
Department of Chemistry, Biochemistry, Umeå University, Umeå, Sweden.
Linköping University, Department of Clinical and Experimental Medicine, Medical Microbiology. Linköping University, Faculty of Health Sciences.
Department of Odontology, Umeå University, Umeå, Sweden.
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology.
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2002 (English)In: Biochimica et Biophysica Acta - Proteins and Proteomics, ISSN 1570-9639, E-ISSN 1878-1454, Vol. 1601, no 2, 192-199 p.Article in journal (Refereed) Published
Abstract [en]

Helicobacter pylori, the causative agent of peptic ulcer disease, expresses two different forms of the zinc-containing enzyme carbonic anhydrase (CA) (α and β), catalyzing the reversible hydration of CO2. Presumably, the high CO2 requirement of H. pylori implies an important role for this enzyme in the bacterial physiology. In this paper, expression of the CAs has been analyzed in three different strains of the bacterium, 26695, J99 and 17.1, and appears to be independent of CO2 concentration in the investigated range (0.1–10%). Presence of the potent and highly specific CA inhibitor, acetazolamide, in the medium does not seem to inhibit bacterial growth at the given sulfonamide concentration. Moreover, the localization and distribution of the α-CA was analyzed by immunonegative staining, while SDS-digested freeze-fracture immunogold labelling was used for the β-form of the enzyme. The latter method has the advantage of allowing assessment of protein localization to distinct cell compartments and membrane structures. The resulting electron microscopy images indicate a localization of the β-CA in the cytosol, on the cytosolic side of the inner membrane and on the outer membrane facing the periplasmic space. The α-enzyme was found attached to the surface of the bacterium.

Place, publisher, year, edition, pages
2002. Vol. 1601, no 2, 192-199 p.
Keyword [en]
Carbonic anhydrase, Expression, Localization
National Category
Engineering and Technology
URN: urn:nbn:se:liu:diva-46779DOI: 10.1016/S1570-9639(02)00467-3OAI: diva2:267675
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2012-10-15Bibliographically approved
In thesis
1. Characterisation of surface traits of Helicobacter pylori and their role in the infectious process
Open this publication in new window or tab >>Characterisation of surface traits of Helicobacter pylori and their role in the infectious process
2003 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The surface appendages of bacteria determine the initial contact with host cells. Characterisation of functional organisation and spatial distribution of adhesive traits of outer membrane components of Gram-negative bacteria is a key issue in studies of the parasite-host cell interaction.

With focus on the enteropathogenic Helicobacter pylori, evidenced to cause chronic gastric infections in humans, detergent-digested freeze fracture replica labelling was applied for ultrastructural analyses of envelope distribution of the virulence factors blood group antigen binding adhesin (BabA), and the carbonic anhydrases (α-CA, ß-CA). In a preliminary study the methodology was also used to study the bacteria-host contact between phagocytosing human neutrophils and wild-type H. pylori.

In parallel, bacterial traits were analysed from a molecular and biochemical perspective. This included the specific roles of the BabA and the sialic acid-binding adhesin (SabA), and the neutrophil activating protein (HP-NAP) in neutrophilic stimulation and subsequent inflammatory process. It was concluded that SabA is crucial in the initiation of a neutrophilic response in the mediated inflammation.

This thesis has demonstrated the synergistic application of ultrastructural, molecular and cellular microbiology tools for delineating complex patterns in bacteria-host interactions, thus utilising the well-characterised and clinically important human pathogen H. pylori. This approach could be applicable to other Gram-negative species to clarify known and discern new virulence mechanisms in the multifaceted field of bacterial pathogenesis and bacterial interactions with human host cells.

Place, publisher, year, edition, pages
Linköping: Linköpings universitet, 2003. 77 p.
Linköping University Medical Dissertations, ISSN 0345-0082 ; 805
National Category
Medical and Health Sciences
urn:nbn:se:liu:diva-26665 (URN)11231 (Local ID)91-7373-490-X (ISBN)11231 (Archive number)11231 (OAI)
Public defence
2003-10-03, Elsa Brändströmsalen, Hälsouniversitetet, Linköping, 09:00 (Swedish)
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2012-10-15Bibliographically approved

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Petersson, ChristofferJonsson, Bengt-Harald
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Medical MicrobiologyFaculty of Health SciencesChemistryThe Institute of Technology
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