ArticleJournal of medical microbiology2007
A Helicobacter hepaticus catalase mutant is hypersensitive to oxidative stress and suffers increased DNA damage.
Article in Journal of medical microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Dual RNA sequencing ofmSystems · 2024Article
- Oxidative and nitrosative stress defences of Helicobacter and Campylobacter species that counteract mammalian immunity.FEMS microbiology reviews · 2016Article
- Association between Helicobacter spp. infections and hepatobiliary malignancies: a review.World journal of gastroenterology · 2015Review
- XRCC7 rs#7003908 Polymorphism and Helicobacter pylori Infection-Related Gastric Antrum Adenocarcinoma.International journal of genomics · 2013Article
- Alkyl hydroperoxide reductase is required for Helicobacter cinaedi intestinal colonization and survival under oxidative stress in BALB/c and BALB/c interleukin-10-/- mice.Infection and immunity · 2012Article
- PerR controls peroxide- and iron-responsive expression of oxidative stress defense genes in Helicobacter hepaticus.European journal of microbiology & immunology · 2011Article
- Helicobacter hepaticus infection in mice: models for understanding lower bowel inflammation and cancer.Mucosal immunology · 2011Review
- Evolution of catalases from bacteria to humans.Antioxidants & redox signaling · 2008Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Catalase (KatA) is known to play an important role in oxidative stress resistance in many bacterial species and a homologue exists in Helicobacter hepaticus, a member of the enterohepatic Helicobacter species. Here, a katA mutant was constructed by insertional mutagenesis and its oxidative stress phenotype was investigated. Catalase activity was readily detected [196 units (mg protein crude cell extract)(-1)] in the wild-type, whereas the mutant strain was deficient in, but not devoid of, activity. In contrast, Helicobacter pylori katA strains lack detectable catalase activity and wild-type H. pylori generally contains higher specific activity than H. hepaticus. Wild-type H. hepaticus cells tolerated 6 % O2 for growth, whilst the katA mutant could not survive at this oxygen level. Even at the optimal O2 level, the growth of the H. hepaticus katA strain was severely inhibited, which is also in contrast to H. pylori katA strains. Wild-type H. hepaticus cells withstood exposure to 100 mM H(2)O(2) but the katA mutant cells were killed by the same treatment. Wild-type cells suffered no significant DNA damage by H(2)O(2) treatment (100 mM for 6 min), whilst the same treatment resulted in severe DNA fragmentation in the katA mutant. Thus H. hepaticus KatA plays an important role as an antioxidant protein.
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Registered trials
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