- Helicobacter pylori Proteins Response to Nitric Oxide Stress
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Wei Qu , Yabin Zhou , Chunhong Shao , Yundong Sun , Qunye Zhang , Chunyan Chen , Jihui Jia
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J. Microbiol. 2009;47(4):486-493. Published online September 9, 2009
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DOI: https://doi.org/10.1007/s12275-008-0266-0
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Helicobacter pylori is a highly pathogenic microorganism with various strategies to evade human immune responses. Nitric oxide (NO) and reactive nitrogen species (RNS) generated via nitric oxide synthase pathway are important effectors during the innate immune response. However, the mechanisms of H. pylori to survive the nitrosative stress are not clear. Here the proteomic approach has been used to define the adaptive response of H. pylori to nitrosative stress. Proteomic analysis showed that 38 protein spots were regulated by NO donor, sodium nitroprusside (SNP). These proteins were involved in protein processing, antioxidation, general stress response, and virulence, as well as some unknown functions. Particularly, some of them were participated in iron metabolism, potentially under the control of ferric uptake regulator (Fur). Real time PCR revealed that fur was induced under nitrosative stress, consistent with our deduction. One stress-related protein up-regulated under nitrosative conditions was thioredoxin reductase (TrxR). Inactivation of fur or trxR can lead to increased susceptivity to nitrosative stress respectively. These studies described the adaptive response of H. pylori to nitric oxide stress, and analyzed the relevant role of Fur regulon and TrxR in nitrosative stress management.
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Citations
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- The Changes of Proteomes Components of Helicobacter pylori in Response to Acid Stress without Urea
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Chunhong Shao , Qunye Zhang , Wei Tang , Wei Qu , Yabin Zhou , Yundong Sun , Han Yu , Jihui Jia
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J. Microbiol. 2008;46(3):331-337. Published online July 5, 2008
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DOI: https://doi.org/10.1007/s12275-008-0062-x
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Abstract
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Acid stress is the most obvious challenge Helicobacter pylori encounters in human stomach. The urease system is the basic process used to maintain periplasmic and cytoplasmic pH near neutrality when H. pylori is exposed to acidic condition. However, since the urea concentration in gastric juice is approximately 1 mM, considered possibly insufficient to ensure the survival of H. pylori, it is postulated that additional mechanisms of pH homeostasis may contribute to the acid adaptation in H. pylori. In order to identify the acid-related proteins other than the urease system we have compared the proteome profiles of H. pylori strain 26695 exposed to different levels of external pH (7.4, 6.0, 5.0, 4.0, 3.0, and 2.0) for 30 min in the absence of urea using 2-DE. Differentially expressed proteins were identified by MALDI-TOF-TOF-MS analysis, which turned out to be 36 different proteins. The functions of these proteins included ammonia production, molecular chaperones, energy metabolism, cell envelope, response regulator and some proteins with unknown function. SOM analysis indicated that H. pylori responds to acid stress through multi-mechanisms involving many proteins, which depend on the levels of acidity the cells encounter.
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The Journal of Microbiology.2011; 49(2): 251. CrossRef - Virulence factor cytotoxin-associated gene A in Helicobacter pylori is downregulated by interferon-γin vitro
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The Journal of Microbiology.2009; 47(4): 486. CrossRef
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