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The functional and catalytic landscape of urease reveals a conserved target against Helicobacter pylori.

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Τίτλος: The functional and catalytic landscape of urease reveals a conserved target against Helicobacter pylori.
Συγγραφείς: Song Q; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), School of Life Sciences, Southwest University, Chongqing, People's Republic of China.; Chongqing Municipality Clinical Research Center for Endocrinology and Metabolic Diseases, Chongqing University Three Gorges Hospital, Chongqing, People's Republic of China., Wu H; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China., Ma Z; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), School of Life Sciences, Southwest University, Chongqing, People's Republic of China., Huang T; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China., Zhu X; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China., Zhang Z; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China., Wu G; Chongqing Municipality Clinical Research Center for Endocrinology and Metabolic Diseases, Chongqing University Three Gorges Hospital, Chongqing, People's Republic of China., Manzoor R; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China., Liu S; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China., Wang Y; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China., Li X; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China., Zhang W; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), School of Life Sciences, Southwest University, Chongqing, People's Republic of China.; Chongqing Municipality Clinical Research Center for Endocrinology and Metabolic Diseases, Chongqing University Three Gorges Hospital, Chongqing, People's Republic of China., Ye X; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), School of Life Sciences, Southwest University, Chongqing, People's Republic of China., Ma H; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China.
Πηγή: Gut microbes [Gut Microbes] 2026 Dec 31; Vol. 18 (1), pp. 2653575. Date of Electronic Publication: 2026 Apr 03.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Taylor & Francis Country of Publication: United States NLM ID: 101495343 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1949-0984 (Electronic) Linking ISSN: 19490976 NLM ISO Abbreviation: Gut Microbes Subsets: MEDLINE
Imprint Name(s): Publication: 2015- : Philadelphia, PA : Taylor & Francis
Original Publication: Austin, Tex. : Landes Bioscience
Ιατρικοί όροι (MeSH): Urease*/metabolism , Urease*/genetics , Urease*/antagonists & inhibitors , Urease*/chemistry , Helicobacter pylori*/enzymology , Helicobacter pylori*/drug effects , Helicobacter pylori*/genetics , Helicobacter pylori*/pathogenicity , Anti-Bacterial Agents*/pharmacology , Bacterial Proteins*/genetics , Bacterial Proteins*/metabolism , Bacterial Proteins*/antagonists & inhibitors , Bacterial Proteins*/chemistry, Helicobacter Infections/microbiology ; Helicobacter Infections/drug therapy ; Enzyme Inhibitors/pharmacology ; Humans ; Drug Resistance, Bacterial ; Catalytic Domain
Περίληψη: Nearly half of the global population is infected with Helicobacter pylori. Antibiotic use has led to substantial antimicrobial resistance and unintended gut microbiota depletion, creating an urgent need for alternative therapeutic strategies. Here, we demonstrate that urease, a key enzyme that enables H. pylori survival by hydrolysing urea to neutralize stomach acid, is a conserved antibacterial target with low risk of resistance development. Using comprehensive deep mutational scanning coupled with phage-based functional screening, we systematically evaluated how mutations in core residues affect urease expression, enzymatic activity, bacterial colonization, and virulence, uncovering the catalytic nature of H. pylori urease. We found exceptional evolutionary conservation within the urease catalytic pocket, and potential mutation sites that affect urease activity are not close to the core of this pocket. Analysis of existing urease inhibitors revealed that their binding sites are not typically in these potential mutation sites, which indicates that the potential for resistance development is low. In addition, we show that targeting urease alone is effective in eradicating H. pylori and synergistically boosts the efficacy of antibiotics. Notably, the incorporation of urease inhibitors into antibiotic-based therapeutic regimens effectively preserves gut microbiota diversity and microbial genomic stability, thereby lowering the risk of antibiotic resistance. Collectively, our study elucidate the inherent resistance-resistant property of urease and establish the clinical value of combining urease inhibitors with antibiotics to reduce antibiotic resistance.
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Nat Commun. 2020 Oct 9;11(1):5101. (PMID: 33037208)
Avian Pathol. 2015;44(3):162-8. (PMID: 25690020)
Curr Med Chem. 2002 Jul;9(14):1323-48. (PMID: 12132990)
Chem Rec. 2022 Aug;22(8):e202200026. (PMID: 35502852)
Int J Mol Sci. 2023 Dec 15;24(24):. (PMID: 38139349)
J Gastroenterol. 1998;33 Suppl 10:53-6. (PMID: 9840019)
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Clin Chem. 2009 Apr;55(4):611-22. (PMID: 19246619)
J Antimicrob Chemother. 1997 Oct;40(4):551-9. (PMID: 9372425)
Expert Opin Ther Pat. 2019 Mar;29(3):181-189. (PMID: 30776929)
Curr Med Chem. 2020;27(23):3967-3982. (PMID: 30827224)
Molecules. 2023 Mar 16;28(6):. (PMID: 36985670)
Clin Microbiol Rev. 2012 Jul;25(3):545-82. (PMID: 22763637)
Am J Gastroenterol. 2024 Sep 1;119(9):1730-1753. (PMID: 39626064)
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Helicobacter. 2018 Apr;23(2):e12475. (PMID: 29512258)
N Engl J Med. 2019 Mar 21;380(12):1158-1165. (PMID: 30893536)
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Contributed Indexing: Keywords: Helicobacter pylori; antibiotic resistance; gut microbiota; mutation; urease
Substance Nomenclature: EC 3.5.1.5 (Urease)
0 (Anti-Bacterial Agents)
0 (Enzyme Inhibitors)
0 (Bacterial Proteins)
Entry Date(s): Date Created: 20260403 Date Completed: 20260714 Latest Revision: 20260926
Update Code: 20260926
PubMed Central ID: PMC13051613
DOI: 10.1080/19490976.2026.2653575
PMID: 41933291
Βάση Δεδομένων: MEDLINE
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  Data: The functional and catalytic landscape of urease reveals a conserved target against Helicobacter pylori.
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  Data: <searchLink fieldCode="AU" term="%22Song+Q%22">Song Q</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), School of Life Sciences, Southwest University, Chongqing, People's Republic of China.; Chongqing Municipality Clinical Research Center for Endocrinology and Metabolic Diseases, Chongqing University Three Gorges Hospital, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Wu+H%22">Wu H</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Ma+Z%22">Ma Z</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), School of Life Sciences, Southwest University, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Huang+T%22">Huang T</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Zhu+X%22">Zhu X</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Zhang+Z%22">Zhang Z</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Wu+G%22">Wu G</searchLink>; Chongqing Municipality Clinical Research Center for Endocrinology and Metabolic Diseases, Chongqing University Three Gorges Hospital, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Manzoor+R%22">Manzoor R</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Liu+S%22">Liu S</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Wang+Y%22">Wang Y</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Li+X%22">Li X</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Zhang+W%22">Zhang W</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), School of Life Sciences, Southwest University, Chongqing, People's Republic of China.; Chongqing Municipality Clinical Research Center for Endocrinology and Metabolic Diseases, Chongqing University Three Gorges Hospital, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Ye+X%22">Ye X</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), School of Life Sciences, Southwest University, Chongqing, People's Republic of China.<br /><searchLink fieldCode="AU" term="%22Ma+H%22">Ma H</searchLink>; Engineering Research Center of Coptis Development and Utilization (Ministry of Education), College of Pharmaceutical Sciences, Southwest University, Chongqing, People's Republic of China.
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  Data: <searchLink fieldCode="JN" term="%22101495343%22">Gut microbes</searchLink> [Gut Microbes] 2026 Dec 31; Vol. 18 (1), pp. 2653575. <i>Date of Electronic Publication: </i>2026 Apr 03.
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  Data: <searchLink fieldCode="MM" term="%22Urease%22">Urease*</searchLink>/<searchLink fieldCode="MM" term="%22Urease+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Urease%22">Urease*</searchLink>/<searchLink fieldCode="MM" term="%22Urease+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Urease%22">Urease*</searchLink>/<searchLink fieldCode="MM" term="%22Urease+antagonists+%26+inhibitors%22">antagonists & inhibitors</searchLink> <br /><searchLink fieldCode="MM" term="%22Urease%22">Urease*</searchLink>/<searchLink fieldCode="MM" term="%22Urease+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Helicobacter+pylori%22">Helicobacter pylori*</searchLink>/<searchLink fieldCode="MM" term="%22Helicobacter+pylori+enzymology%22">enzymology</searchLink> <br /><searchLink fieldCode="MM" term="%22Helicobacter+pylori%22">Helicobacter pylori*</searchLink>/<searchLink fieldCode="MM" term="%22Helicobacter+pylori+drug+effects%22">drug effects</searchLink> <br /><searchLink fieldCode="MM" term="%22Helicobacter+pylori%22">Helicobacter pylori*</searchLink>/<searchLink fieldCode="MM" term="%22Helicobacter+pylori+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Helicobacter+pylori%22">Helicobacter pylori*</searchLink>/<searchLink fieldCode="MM" term="%22Helicobacter+pylori+pathogenicity%22">pathogenicity</searchLink> <br /><searchLink fieldCode="MM" term="%22Anti-Bacterial+Agents%22">Anti-Bacterial Agents*</searchLink>/<searchLink fieldCode="MM" term="%22Anti-Bacterial+Agents+pharmacology%22">pharmacology</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+antagonists+%26+inhibitors%22">antagonists & inhibitors</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+chemistry%22">chemistry</searchLink><br /><searchLink fieldCode="MH" term="%22Helicobacter+Infections%22">Helicobacter Infections</searchLink>/<searchLink fieldCode="MH" term="%22Helicobacter+Infections+microbiology%22">microbiology</searchLink> ; <searchLink fieldCode="MH" term="%22Helicobacter+Infections%22">Helicobacter Infections</searchLink>/<searchLink fieldCode="MH" term="%22Helicobacter+Infections+drug+therapy%22">drug therapy</searchLink> ; <searchLink fieldCode="MH" term="%22Enzyme+Inhibitors%22">Enzyme Inhibitors</searchLink>/<searchLink fieldCode="MH" term="%22Enzyme+Inhibitors+pharmacology%22">pharmacology</searchLink> ; <searchLink fieldCode="MH" term="%22Humans%22">Humans</searchLink> ; <searchLink fieldCode="MH" term="%22Drug+Resistance%2C+Bacterial%22">Drug Resistance, Bacterial</searchLink> ; <searchLink fieldCode="MH" term="%22Catalytic+Domain%22">Catalytic Domain</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Nearly half of the global population is infected with Helicobacter pylori. Antibiotic use has led to substantial antimicrobial resistance and unintended gut microbiota depletion, creating an urgent need for alternative therapeutic strategies. Here, we demonstrate that urease, a key enzyme that enables H. pylori survival by hydrolysing urea to neutralize stomach acid, is a conserved antibacterial target with low risk of resistance development. Using comprehensive deep mutational scanning coupled with phage-based functional screening, we systematically evaluated how mutations in core residues affect urease expression, enzymatic activity, bacterial colonization, and virulence, uncovering the catalytic nature of H. pylori urease. We found exceptional evolutionary conservation within the urease catalytic pocket, and potential mutation sites that affect urease activity are not close to the core of this pocket. Analysis of existing urease inhibitors revealed that their binding sites are not typically in these potential mutation sites, which indicates that the potential for resistance development is low. In addition, we show that targeting urease alone is effective in eradicating H. pylori and synergistically boosts the efficacy of antibiotics. Notably, the incorporation of urease inhibitors into antibiotic-based therapeutic regimens effectively preserves gut microbiota diversity and microbial genomic stability, thereby lowering the risk of antibiotic resistance. Collectively, our study elucidate the inherent resistance-resistant property of urease and establish the clinical value of combining urease inhibitors with antibiotics to reduce antibiotic resistance.
– Name: Ref
  Label: References
  Group: RefInfo
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– Name: SubjectMinor
  Label: Contributed Indexing
  Group:
  Data: <i>Keywords: </i>Helicobacter pylori; antibiotic resistance; gut microbiota; mutation; urease
– Name: NumberCAS
  Label: Substance Nomenclature
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  Data: EC 3.5.1.5 (Urease)<br />0 (Anti-Bacterial Agents)<br />0 (Enzyme Inhibitors)<br />0 (Bacterial Proteins)
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  Data: <i>Date Created: </i>20260403 <i>Date Completed: </i>20260714 <i>Latest Revision: </i>20260926
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  Data: 20260926
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  Data: 10.1080/19490976.2026.2653575
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        Value: 10.1080/19490976.2026.2653575
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        Text: English
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        StartPage: 2653575
    Subjects:
      – SubjectFull: Helicobacter Infections microbiology
        Type: general
      – SubjectFull: Helicobacter Infections drug therapy
        Type: general
      – SubjectFull: Enzyme Inhibitors pharmacology
        Type: general
      – SubjectFull: Humans
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      – SubjectFull: Drug Resistance, Bacterial
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      – SubjectFull: Urease metabolism
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      – SubjectFull: Urease antagonists & inhibitors
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      – SubjectFull: Urease chemistry
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      – SubjectFull: Helicobacter pylori drug effects
        Type: general
      – SubjectFull: Helicobacter pylori genetics
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      – SubjectFull: Helicobacter pylori pathogenicity
        Type: general
      – SubjectFull: Anti-Bacterial Agents pharmacology
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      – SubjectFull: Bacterial Proteins genetics
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      – SubjectFull: Bacterial Proteins chemistry
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    Titles:
      – TitleFull: The functional and catalytic landscape of urease reveals a conserved target against Helicobacter pylori.
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            – D: 31
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              Text: 2026 Dec 31
              Type: published
              Y: 2026
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