Two remarkable serine/leucine polymorphisms in Helicobacter pylori: functional importance for serine protease HtrA and adhesin BabA

Cell Commun Signal. 2024 May 2;22(1):250. doi: 10.1186/s12964-024-01635-5.

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.

Keywords: Adaptation; BabA; Evolution; HtrA; SNP.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial* / genetics
  • Adhesins, Bacterial* / metabolism
  • Animals
  • Helicobacter Infections / genetics
  • Helicobacter Infections / microbiology
  • Helicobacter pylori* / genetics
  • Humans
  • Leucine* / genetics
  • Leucine* / metabolism
  • Polymorphism, Single Nucleotide / genetics
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism
  • Serine* / genetics
  • Serine* / metabolism

Substances

  • Adhesins, Bacterial
  • Serine
  • Leucine
  • BabA protein, Helicobacter pylori
  • Serine Endopeptidases