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

• Published in: Cell communication and signaling Vol. 22; no. 1; p. 250
• Main Authors: Backert, Steffen, Tegtmeyer, Nicole, Horn, Anselm H C, Sticht, Heinrich, Linz, Bodo
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 02-05-2024; BioMed Central; BMC
• Subjects: ABO system; Adaptation; Adhesins, Bacterial - genetics; Adhesins, Bacterial - metabolism; Amino acids; Animals; Antigens; BabA; Bacteria; Bacterial proteins; Biogeography; Blood group O; Blood groups; Brief Report; Campylobacter; Chromosomes; Enzymes; Evolution; Gastric cancer; Genes; Genetic aspects; Genetic polymorphisms; Genomes; Health aspects; Helicobacter Infections - genetics; Helicobacter Infections - microbiology; Helicobacter pylori; Helicobacter pylori - genetics; HtrA; Humans; Infection; Infections; Kinases; Leucine; Leucine - genetics; Leucine - metabolism; Microbiological research; Mutation; Pathogens; Physiological aspects; Polymorphism; Polymorphism, Single Nucleotide - genetics; Proteins; Serine; Serine - genetics; Serine - metabolism; Serine Endopeptidases - genetics; Serine Endopeptidases - metabolism; Serine proteinase; Single nucleotide polymorphisms; Single-nucleotide polymorphism; SNP; Thrombin; Virulence; Germany; BabA; Evolution; HtrA; SNP; Adaptation
• DOI: 10.1186/s12964-024-01635-5
• EISSN: 1478-811X

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.