Literature DB >> 12368104

Structure of the neutrophil-activating protein from Helicobacter pylori.

Giuseppe Zanotti1, Elena Papinutto, William Dundon, Roberto Battistutta, Michela Seveso, Giuseppe Giudice, Rino Rappuoli, Cesare Montecucco.   

Abstract

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.

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Year:  2002        PMID: 12368104     DOI: 10.1016/s0022-2836(02)00879-3

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  40 in total

1.  Immunogenicity of attenuated measles virus engineered to express Helicobacter pylori neutrophil-activating protein.

Authors:  Ianko D Iankov; Iana H Haralambieva; Evanthia Galanis
Journal:  Vaccine       Date:  2010-12-21       Impact factor: 3.641

2.  Helicobacter pylori SabA adhesin evokes a strong inflammatory response in human neutrophils which is down-regulated by the neutrophil-activating protein.

Authors:  Christoffer Petersson; Maria Forsberg; Marina Aspholm; Farzad O Olfat; Tony Forslund; Thomas Borén; Karl-Eric Magnusson
Journal:  Med Microbiol Immunol       Date:  2006-06-07       Impact factor: 3.402

3.  DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus.

Authors:  Pierpaolo Ceci; Sara Cellai; Elisabetta Falvo; Claudio Rivetti; Gian Luigi Rossi; Emilia Chiancone
Journal:  Nucleic Acids Res       Date:  2004-11-08       Impact factor: 16.971

4.  The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus.

Authors:  Célia V Romão; Edward P Mitchell; Sean McSweeney
Journal:  J Biol Inorg Chem       Date:  2006-07-20       Impact factor: 3.358

Review 5.  Dps-like proteins: structural and functional insights into a versatile protein family.

Authors:  Teemu Haikarainen; Anastassios C Papageorgiou
Journal:  Cell Mol Life Sci       Date:  2009-10-14       Impact factor: 9.261

6.  Effect of the charge distribution along the "ferritin-like" pores of the proteins from the Dps family on the iron incorporation process.

Authors:  Pierpaolo Ceci; Gisa Di Cecca; Mattia Falconi; Francesco Oteri; Carlotta Zamparelli; Emilia Chiancone
Journal:  J Biol Inorg Chem       Date:  2011-05-06       Impact factor: 3.358

7.  Campylobacter jejuni Dps protein binds DNA in the presence of iron or hydrogen peroxide.

Authors:  Luciano F Huergo; Hossinur Rahman; Adis Ibrahimovic; Christopher J Day; Victoria Korolik
Journal:  J Bacteriol       Date:  2013-02-22       Impact factor: 3.490

8.  Helicobacter pylori neutrophil activating protein as target for new drugs against H. pylori inflammation.

Authors:  Theodora Choli-Papadopoulou; Filippos Kottakis; Georgios Papadopoulos; Stefanos Pendas
Journal:  World J Gastroenterol       Date:  2011-06-07       Impact factor: 5.742

Review 9.  Clinical proteomics identifies potential biomarkers in Helicobacter pylori for gastrointestinal diseases.

Authors:  Chun-Hao Huang; Shyh-Horng Chiou
Journal:  World J Gastroenterol       Date:  2014-02-14       Impact factor: 5.742

Review 10.  Structural and functional aspects of the Helicobacter pylori secretome.

Authors:  Giuseppe Zanotti; Laura Cendron
Journal:  World J Gastroenterol       Date:  2014-02-14       Impact factor: 5.742

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