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NapA protects Helicobacter pylori from oxidative stress damage, and its production is influenced by the ferric uptake regulator

¹Institute of Infections and Immunity, Queen's Medical Centre, C-floor West Block, Nottingham NG7 2UH, UK ²Division of Gastroenterology, University Hospital, Nottingham NG7 2UH, UK ³School of Pharmaceutical Sciences, Nottingham University, Nottingham NG7 2RD, UK#dReceived 10 September 2002 Accepted 21 January 2003

Correspondence: Kim Hardie (kim.hardie{at}nottingham.ac.uk)

The Helicobacter pylori protein NapA has been identified as a homologue of the Escherichia coli protein Dps. It is shown in this study that, like Dps, NapA is produced maximally in stationary phase cells and contributes to the ability of H. pylori to survive under oxidative stress conditions. Moreover, NapA co-localizes with the nuclear material, suggesting that it can interact with DNA in vivo. Furthermore, it is demonstrated that repression of NapA production by iron starvation was not so pronounced in a H. pylori fur mutant, suggesting that the ferric uptake regulator (Fur) is involved in napA regulation, and a potential fur box by which this control could be mediated is identified. This finding is consistent with the regulation of iron-binding proteins by Fur and also the modulation of Fur during oxidative stress, thus allowing NapA levels to be increased in the environmental conditions under which its ability to protect DNA from attack by toxic free radicals is most beneficial to the cell.

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