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Proinflammatory activity of a cecropin-like antibacterial peptide from Helicobacter pylori

Journal article
Authors Johan Bylund
T. Christophe
F. Boulay
Thomas Nyström
Anna Karlsson
Claes Dahlgren
Published in Antimicrob Agents Chemother
Volume 45
Issue 6
Pages 1700-4
Publication year 2001
Published at Department of Cell and Molecular Biology
Institute of Internal Medicine, Dept of Rheumatology and Inflammation Research
Pages 1700-4
Language en
Keywords Anti-Bacterial Agents/*pharmacology, Bacterial Proteins/pharmacology, Helicobacter pylori/*drug effects, Humans, Macrophage-1 Antigen/*drug effects, NADPH Oxidase/metabolism, Neutrophil Activation/drug effects, Neutrophils/*drug effects/enzymology, Peptide Fragments/pharmacology, Receptors, Cell Surface/drug effects, *Receptors, Formyl Peptide, *Receptors, Lipoxin
Subject categories Medical and Health Sciences


Helicobacter pylori, the bacterial pathogen associated with gastritis and peptic ulcers, is highly successful in establishing infection in the human gastric mucosa, a process typically associated with massive infiltration of inflammatory cells. Colonization of the mucosa is suggested to be facilitated by H. pylori-produced cecropin-like peptides with antibacterial properties, giving the microbe a competitive advantage over other bacteria. We show that a cecropin-like antibacterial peptide from H. pylori, Hp(2-20), not only has a potent bactericidal effect but also induces proinflammatory activities in human neutrophils, e.g., upregulation of integrins (Mac-1), induction of chemotaxis, and activation of the oxygen radical producing NADPH-oxidase. Furthermore, we show that these effects are mediated through binding of Hp(2-20) to the promiscuous, G-protein-linked lipoxin A(4) receptor-formyl peptide-like receptor 1.

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