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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Bibliographic Details
Published in:Journal of molecular biology 2002-10, Vol.323 (1), p.125-130
Main Authors: Zanotti, Giuseppe, Papinutto, Elena, Dundon, William G., Battistutta, Roberto, Seveso, Michela, Giudice, Giuseppe Del, Rappuoli, Rino, Montecucco, Cesare
Format: Article
Language:English
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
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Summary: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.
ISSN:0022-2836
1089-8638
DOI:10.1016/S0022-2836(02)00879-3