پاسخ : آنزیم urease در Helicobacter pylori !
All ureases contain two nickel ions in each of their active sites; H. pylori urease appears to have six active sites and, thus, 12 nickel ions. To overcome the nickel limitation that probably occurs in the host, H. pylori has developed a high-affinity system to acquire nickel ions. It appears that these ions can be transported into H. pylori by at least two mechanisms.
The first is NixA, a cytoplasmic membrane-bound protein of 36,991 molecular weight, which transports nickel ions with a KT of 11.3 nM (70). E. coli expressing NixA transported nickel ions with a Vmax of 1,750 pmol/min/108 bacteria. Topology studies using 21 phoA and 21 lacZ translational fusions revealed that the protein has eight transmembrane domains and a large periplasmic loop with both the N terminus and C terminus residing in the cytosol (34). Negatively charged Asp and Glu residues and His residues, which are located in the transmembrane domains, were shown to be critical for active transport of nickel ions (33). Two domains have been identified in NixA and the small family of high-affinity nickel transport proteins as essential for transport: GX2HAXDADH in helix II and GX2FX2GHSSVV in helix III (33).
nsertional inactivation of nixA in H. pylori ATCC 43504 resulted in a 69% decrease in the rate of nickel transport and a 42% reduction in urease activity relative to the parent strain (6). These rates varied among strains but are reduced significantly in the nixA mutants. The fact that nickel transport or urease activity is not totally abolished in these mutants supports the presence of a
second mechanism of nickel transport that has yet to be elucidated.
When a nixA mutant of H. pylori SS1 and the parent strain were mixed and used orogastrically to cochallenge mice, the nixA mutant was never recovered by culture of gastric tissue (77). That is, the wild-type always outcompeted the nixA mutant. Interestingly, however, the nixA mutant was able to colonize the gastric mucosa of mice when inoculated alone (i.e., in the absence of the wild type), and the CFU per gram of stomach approached levels achieved in mice infected with the parental strain. These studies indicated that NixA-mediated nickel transport provides a selective advantage for H. pylori in the gastric mucosa.
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http://www.ncbi.nlm.nih.gov/books/NBK2417/
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