Structure of the neutrophil-activating protein from Helicobacter pylori

被引：130

作者：

Zanotti, G

Papinutto, E

Dundon, WG

Battistutta, R

Seveso, M

Del Giudice, G

Rappuoli, R

Montecucco, C

机构：

[1] Univ Padua, Dipartimento Chim Organ, I-35131 Padua, Italy

[2] Univ Padua, Ctr Biopolimeri, CNR, I-35131 Padua, Italy

[3] Venetian Inst Mol Med, I-35129 Padua, Italy

[4] Univ Padua, CNR, Ctr Biomembrane, I-35121 Padua, Italy

[5] Univ Padua, CNR, Dipartimento Sci Biomed, I-35121 Padua, Italy

[6] CHIRON Res Labs, I-53100 Siena, Italy

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2002年 / 323卷 / 01期

关键词：

neutrophil-activating protein; Helicobacter pylori; iron storage; ferritins; crystal structure;

D O I：

10.1016/S0022-2836(02)00879-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：125 / 130

页数：6

共 24 条

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