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Structure of the Neutrophil-activating Protein from Helicobacter pylori
Helicobacter pylori is a major human pathogen associated with severe gastroduodenal diseases, including ulcers and cancers. An H. pylori protein that is highly immunogenic in humans and mice has been identified recently. This protein has been termed HP-NAP, due to its ability of activating neutrophi...
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Published in: | Journal of molecular biology 2002-10, Vol.323 (1), p.125-130 |
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container_title | Journal of molecular biology |
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creator | Zanotti, Giuseppe Papinutto, Elena Dundon, William G. Battistutta, Roberto Seveso, Michela Giudice, Giuseppe Del Rappuoli, Rino Montecucco, Cesare |
description | Helicobacter pylori is a major human pathogen associated with severe gastroduodenal diseases, including ulcers and cancers. An
H.
pylori
protein that is highly immunogenic in humans and mice has been identified recently. This protein has been termed HP-NAP, due to its ability of activating neutrophils. In order to achieve a molecular understanding of its unique immunogenic and pro-inflammatory properties, we have determined its three-dimensional structure. Its quaternary structure is similar to that of the dodecameric bacterial ferritins (Dps-like family), but it has a different surface potential charge distribution. This is due to the presence of a large number of positively charged residues, which could well account for its unique ability in activating human leukocytes. |
doi_str_mv | 10.1016/S0022-2836(02)00879-3 |
format | article |
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H.
pylori
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H.
pylori
protein that is highly immunogenic in humans and mice has been identified recently. This protein has been termed HP-NAP, due to its ability of activating neutrophils. In order to achieve a molecular understanding of its unique immunogenic and pro-inflammatory properties, we have determined its three-dimensional structure. Its quaternary structure is similar to that of the dodecameric bacterial ferritins (Dps-like family), but it has a different surface potential charge distribution. 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H.
pylori
protein that is highly immunogenic in humans and mice has been identified recently. This protein has been termed HP-NAP, due to its ability of activating neutrophils. In order to achieve a molecular understanding of its unique immunogenic and pro-inflammatory properties, we have determined its three-dimensional structure. Its quaternary structure is similar to that of the dodecameric bacterial ferritins (Dps-like family), but it has a different surface potential charge distribution. This is due to the presence of a large number of positively charged residues, which could well account for its unique ability in activating human leukocytes.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>12368104</pmid><doi>10.1016/S0022-2836(02)00879-3</doi><tpages>6</tpages></addata></record> |
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source | ScienceDirect Freedom Collection |
subjects | Bacterial Proteins - chemistry Bacterial Proteins - physiology crystal structure ferritins Helicobacter pylori Helicobacter pylori - chemistry iron storage Models, Molecular Neutrophil Activation - physiology neutrophil-activating protein Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - metabolism |
title | Structure of the Neutrophil-activating Protein from Helicobacter pylori |
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