4.4 Article

Expansion of nickel binding- and histidine-rich proteins during gastric adaptation of Helicobacter species

期刊

METALLOMICS
卷 14, 期 9, 页码 -

出版社

OXFORD UNIV PRESS
DOI: 10.1093/mtomcs/mfac060

关键词

Histidine-rich proteins; metal binding proteins; phylogenetics; Helicobacter pylori; nickel; urease

资金

  1. Institut Pasteur [73-17]
  2. IdEx Unistra [ANR (agence nationale de la recherche)] [10-IDEX-0002]
  3. SFRI-STRAT'US project [ANR 20-SFRI-0012]
  4. EUR IMCBio [ANR17-EURE-0023]
  5. European EPIC-XS project - Horizon 2020 program of the European Union [823839]

向作者/读者索取更多资源

Acquisition and homeostasis of essential metals during host colonization by bacterial pathogens rely on metal uptake, trafficking, and storage proteins. How these factors have evolved within bacterial pathogens is poorly defined. In this study, the researchers analyzed histidine-rich proteins (HRPs) among 39 Epsilonproteobacteria to investigate their role in gastric colonization by Helicobacter spp. They found that gastric Helicobacter spp. have an expanded repertoire of HRPs, particularly those with C-terminal histidine-rich domains, which may be associated with the presence of the essential nickel enzyme urease. This HRP expansion is believed to be associated with the unique properties of these organisms that require large amounts of intracellular nickel for survival.
Acquisition and homeostasis of essential metals during host colonization by bacterial pathogens rely on metal uptake, trafficking, and storage proteins. How these factors have evolved within bacterial pathogens is poorly defined. Urease, a nickel enzyme, is essential for Helicobacter pylori to colonize the acidic stomach. Our previous data suggest that acquisition of nickel transporters and a histidine-rich protein (HRP) involved in nickel storage in H. pylori and gastric Helicobacter spp. have been essential evolutionary events for gastric colonization. Using bioinformatics, proteomics, and phylogenetics, we extended this analysis to determine how evolution has framed the repertoire of HRPs among 39 Epsilonproteobacteria; 18 gastric and 11 non-gastric enterohepatic (EH) Helicobacter spp., as well as 10 other Epsilonproteobacteria. We identified a total of 213 HRPs distributed in 22 protein families named orthologous groups (OGs) with His-rich domains, including 15 newly described OGs. Gastric Helicobacter spp. are enriched in HRPs (7.7 +/- 1.9 HRPs/strain) as compared to EH Helicobacter spp. (1.9 +/- 1.0 HRPs/strain) with a particular prevalence of HRPs with C-terminal histidine-rich domains in gastric species. The expression and nickel-binding capacity of several HRPs was validated in five gastric Helicobacter spp. We established the evolutionary history of new HRP families, such as the periplasmic HP0721-like proteins and the HugZ-type heme oxygenases. The expansion of histidine-rich extensions in gastric Helicobacter spp. proteins is intriguing but can tentatively be associated with the presence of the urease nickel enzyme. We conclude that this HRP expansion is associated with unique properties of organisms that rely on large intracellular nickel amounts for their survival.

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