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Expression and localization of α- and β-carbonic anhydrase in Helicobacter pylori
Umeå University, Faculty of Science and Technology, Department of Chemistry.
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2002 (English)In: Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, Vol. 1601, no 2, 192-9 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, 192-9 p.
Keyword [en]
Expression, Localization, Carbonic anhydrase, Enzyme, carbonic anhydrase (EC
URN: urn:nbn:se:umu:diva-8785DOI: doi:10.1016/S1570-9639(02)00467-3OAI: diva2:148456
Available from: 2008-02-12 Created: 2008-02-12 Last updated: 2011-03-30Bibliographically approved

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Borén, ThomasLindskog, Sven
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