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- W2081618970 abstract "H. pilory is a Gram-negative bacterium that colonizes the stomach of probably half of the human population. It is associated with gastritis, peptic ulcers and mucosa-associated lymphoid tissue lymphomas. Many factors contribute to the virulence of H. pylori [1]. Among them, the enzyme urease, the Neutrophil Activating Protein, NAP [2] and the secreted protein toxin VacA. However, the major genetic difference in HP isolates is the presence or absence of a specific pathogenicity island, named cag-PAI. It is a 40-kb locus that contains about 30 ORFs, whose function is unknown, with few exceptions. We have cloned, expressed, and purified several proteins of the cag pathogenicity island of H. pylori. They all have been expressed in E. coli. We have already solved the structure of CagZ, using the SeMet method [3] and the structure will be described in detail. We have also obtained crystals of a second protein, CagS, and its structure determination is in progress, along with crystallization tests on other cag proteins. Our final goal is to determine, in collaboration with other groups [4], most of the proteins coded by the cag-PAI island." @default.
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- W2081618970 date "2005-08-23" @default.
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- W2081618970 title "Structural proteomics of proteins coded by the<i>cag</i>PAI of<i>Helicobacter pylori</i>" @default.
- W2081618970 doi "https://doi.org/10.1107/s0108767305088975" @default.
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