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Identification and molecular analysis of superoxide dismutase isoforms in Helicobacter pylori
Authors:Bereswill S  Neuner O  Strobel S  Kist M
Institution:University of Freiburg, Institute of Medical Microbiology and Hygiene, Department of Microbiology and Hygiene, Hermann-Herder-Str. 11, D-79104, Freiburg, Germany. bereswil@sun11.ukl.uni-freiburg.de
Abstract:Three electromorphs of iron superoxide dismutase (FeSOD) were identified among 29 Helicobacter pylori isolates by native gel electrophoresis and activity staining. The electromorphs designated isoforms A, B, and C are characterized by slow, intermediate and fast electrophoretic migration, respectively, which was not observed under denaturing conditions. The isoforms were not associated with virulence determinants and with the outcome of disease. Sequence analysis of the sodB gene in strains producing different FeSOD isoforms and comparison of deduced protein sequences revealed that differences in the electric migration behavior are associated with exchange of charged amino acids, suggesting that faster migration is caused by a more negative total charge of the proteins. Electrophoretic migration of native FeSOD was not influenced by changes in the iron cofactor concentration, oxidative stress, and different media, indicating that FeSOD isoforms represent stable strain-specific markers.
Keywords:Helicobacter pylori            Iron-cofactored superoxide dismutase  SodB  Iron regulation
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