Author(s): Birkholz S, Knipp U, Lemma E, Krger A, Opferkuch W
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Abstract An immunogenic protein with an apparent mol. wt of 80 kDa that was recognised by 55\% of sera from patients infected with Helicobacter pylori in Western blots was found in butanol extracts of H. pylori membranes. The N-terminal amino-acid sequence of the 80-kDa protein showed 80\% identity with the N-terminal sequence of subunit A of the fumarate reductase of Wolinella succinogenes, suggesting the existence of a fumarate reductase in H. pylori. The membrane fraction of H. pylori catalysed succinate oxidation with methylene blue at a specific enzyme activity of 0.06 U/mg of protein. The enzyme was purified by Triton X100 extraction followed by ion-exchange chromatography. The purified enzyme contained an 80-kDa protein which was recognised by rabbit serum raised against subunit A of fumarate reductase of W. succinogenes. A second protein band with a mol. wt of 31 kDa was recognised by rabbit serum raised against subunit B of fumarate reductase of W. succinogenes. Two-dimensional gel electrophoresis demonstrated that the 80- and 31-kDa proteins were subunits of one protein complex. These results indicate that H. pylori contains an enzyme that is very similar to W. succinogenes fumarate reductase. The 80-kDa subunit was recognised in sonicates of all 32 H. pylori strains tested by rabbit antibodies raised against subunit A of fumarate reductase of W. succinogenes, indicating that fumarate reductase is a common protein in H. pylori. The fumarate reductase of H. pylori might enable the bacterium to perform anaerobic respiration in a similar fashion to other anaerobic or facultative bacteria.
This article was published in J Med Microbiol
and referenced in General Medicine: Open Access