Article (Scientific journals)
Ir-LBP, an ixodes ricinus tick salivary LTB4-binding lipocalin, interferes with host neutrophil function.
Beaufays, Jérôme; Adam, Benoit; Menten, Catherine et al.
2008In PLoS ONE, 3 (12), p. 3987
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Keywords :
Amino Acid Sequence; Animals; Animals, Genetically Modified; Computer Simulation; Female; Host-Parasite Interactions/genetics/immunology; Ixodes/immunology/metabolism; Leukotriene B4/metabolism; Lipocalins/genetics/metabolism/physiology; Models, Molecular; Molecular Sequence Data; Neutrophil Activation/physiology; Neutrophils/physiology; Protein Binding; Rabbits; Receptors, Leukotriene B4/chemistry/genetics/metabolism/physiology; Salivary Proteins and Peptides/genetics/metabolism/physiology; Sequence Homology, Amino Acid; Tick Infestations/immunology
Abstract :
[en] BACKGROUND: During their blood meal, ticks secrete a wide variety of proteins that can interfere with their host's defense mechanisms. Among these proteins, lipocalins play a major role in the modulation of the inflammatory response. METHODOLOGY/PRINCIPAL FINDINGS: We previously identified 14 new lipocalin genes in the tick Ixodes ricinus. One of them codes for a protein that specifically binds leukotriene B4 with a very high affinity (Kd: +/-1 nM), similar to that of the neutrophil transmembrane receptor BLT1. By in silico approaches, we modeled the 3D structure of the protein and the binding of LTB4 into the ligand pocket. This protein, called Ir-LBP, inhibits neutrophil chemotaxis in vitro and delays LTB4-induced apoptosis. Ir-LBP also inhibits the host inflammatory response in vivo by decreasing the number and activation of neutrophils located at the tick bite site. Thus, Ir-LBP participates in the tick's ability to interfere with proper neutrophil function in inflammation. CONCLUSIONS/SIGNIFICANCE: These elements suggest that Ir-LBP is a "scavenger" of LTB4, which, in combination with other factors, such as histamine-binding proteins or proteins inhibiting the classical or alternative complement pathways, permits the tick to properly manage its blood meal. Moreover, with regard to its properties, Ir-LBP could possibly be used as a therapeutic tool for illnesses associated with an increased LTB4 production.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Beaufays, Jérôme ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Adam, Benoit
Menten, Catherine ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Histologie humaine
Fievez, Laurence ;  Université de Liège - ULiège > Département de sciences fonctionnelles > GIGA-R : Biochimie et biologie moléculaire
Grosjean, Amelie
Decrem, Yves
Prevot, Pierre-Paul
Santini, Sebastien
Brasseur, Robert ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Brossard, Michel
Vanhaeverbeek, Michel
Bureau, Fabrice ;  Université de Liège - ULiège > Département de sciences fonctionnelles > GIGA-R : Biochimie et biologie moléculaire
Heinen, Ernst ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Histologie humaine
Lins, Laurence  ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Vanhamme, Luc
Godfroid, Edmond
More authors (6 more) Less
Language :
English
Title :
Ir-LBP, an ixodes ricinus tick salivary LTB4-binding lipocalin, interferes with host neutrophil function.
Publication date :
2008
Journal title :
PLoS ONE
eISSN :
1932-6203
Publisher :
Public Library of Science, San Franscisco, United States - California
Volume :
3
Issue :
12
Pages :
e3987
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 23 June 2010

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