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Two remarkable serine/leucine polymorphisms in Helicobacter pylori: functional importance for serine protease HtrA
Steffen Backert1, Nicole Tegtmeyer2, Anselm H C Horn3
1Department Biology, Division of Microbiology, Friedrich-Alexander Universität Erlangen-Nürnberg, Staudtstr. 5, Erlangen, 91058, Germany. steffen.backert@fau.de.
Abstract:
Single nucleotide polymorphisms (SNPs) account for significant genomic variability in microbes, including the highly diverse gastric pathogen Helicobacter pylori. However, data on the effects of specific SNPs in pathogen-host interactions are scarce. Recent functional studies unravelled how a serine/leucine polymorphism in serine protease HtrA affects the formation of proteolytically active trimers and modulates cleavage of host cell-to-cell junction proteins during infection. A similar serine/leucine mutation in the carbohydrate binding domain of the adhesin BabA controls binding of ABO blood group antigens, enabling binding of either only the short Lewis b/H antigens of blood group O or also the larger antigens of blood groups A and B. Here we summarize the functional importance of these two remarkable bacterial SNPs and their effect on the outcome of pathogen-host interactions.
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