title: Accumulation of manganese in Neisseria gonorrhoeae correlates with resistance to oxidative killing by superoxide anion and is independent of superoxide dismutase activity.
abstract: As a facultative aerobe with a high iron requirement and a highly active aerobic respiratory chain, Neisseria gonorrhoeae requires defence systems to respond to toxic oxygen species such as superoxide. It has been shown that supplementation of media with 100 microM Mn(II) considerably enhanced the resistance of this bacterium to oxidative killing by superoxide. This protection was not associated with the superoxide dismutase enzymes of N. gonorrhoeae. In contrast to previous studies, which suggested that some strains of N. gonorrhoeae might not contain a superoxide dismutase, we identified a sodB gene by genome analysis and confirmed its presence in all strains examined by Southern blotting, but found no evidence for sodA or sodC. A sodB mutant showed very similar susceptibility to superoxide killing to that of wild-type cells, indicating that the Fe-dependent SOD B did not have a major role in resistance to oxidative killing under the conditions tested. The absence of a sodA gene indicated that the Mn-dependent protection against oxidative killing was independent of Mn-dependent SOD A. As a sodB mutant also showed Mn-dependent resistance to oxidative killing, then it is concluded that this resistance is independent of superoxide dismutase enzymes. Resistance to oxidative killing was correlated with accumulation of Mn(II) by the bacterium. We hypothesize that this bacterium uses Mn(II) as a chemical quenching agent in a similar way to the already established process in Lactobacillus plantarum. A search for putative Mn(II) uptake systems identified an ABC cassette-type system (MntABC) with a periplasmic-binding protein (MntC). An mntC mutant was shown to have lowered accumulation of Mn(II) and was also highly susceptible to oxidative killing, even in the presence of added Mn(II). Taken together, these data show that N. gonorrhoeae possesses a Mn(II) uptake system that is critical for resistance to oxidative stress.
authors.affiliation: Department of Microbiology and Parasitology, The University of Queensland, Brisbane, QLD 4072, Australia.
authors.forename: H J
authors.initials: HJ
authors.lastname: Tseng
authors.forename: Y
authors.initials: Y
authors.lastname: Srikhanta
authors.forename: A G
authors.initials: AG
authors.lastname: McEwan
authors.forename: M P
authors.initials: MP
authors.lastname: Jennings
mesh_terms: D000975:Antioxidants / Q000378:metabolism / Q000494:pharmacology; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D002455:Cell Division / Q000187:drug effects; D003470:Culture Media; D008345:Manganese / Q000378:metabolism* / Q000494:pharmacology; D009154:Mutation; D009344:Neisseria gonorrhoeae / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D018384:Oxidative Stress; D033902:Periplasmic Binding Proteins; D017386:Sequence Homology, Amino Acid; D013482:Superoxide Dismutase / Q000235:genetics / Q000378:metabolism*; D013481:Superoxides / Q000378:metabolism* / Q000494:pharmacology
chemical_list: D000975:Antioxidants; D001426:Bacterial Proteins; D002352:Carrier Proteins; D003470:Culture Media; C432957:HmcD protein, Haemophilus influenzae; C432956:MntC protein, Neisseria gonorrhoeae; D033902:Periplasmic Binding Proteins; D013481:Superoxides; D008345:Manganese; C087504:SodB protein, Bacteria; D013482:Superoxide Dismutase