Protéine de liaison au lipopolysaccharide

LBP
Structures disponibles
PDB	Recherche d'orthologue: PDBe RCSB
Identifiants PDB
	4M4D
Identifiants
Aliases	LBP
IDs externes	OMIM: 151990 MGI: 1098776 HomoloGene: 3055 GeneCards: LBP
Position du gène (Homme)
Chr.	Chromosome 20 humain
Fin	38,377,013 bp
Position du gène (Souris)
Chr.	Chromosome 2 (souris)
Fin	158,174,772 bp
Expression génétique
	Fortement exprimé dans
	right lobe of liver; ; muscle tibial antérieur; ; muscle gastrocnémien; ; appendice iléo-cæcal; ; muscle deltoïde; ; subcutaneous adipose tissue; ; right lobe of thyroid gland; ; péricarde; ; rein; ; membrane synoviale;
	Fortement exprimé dans
	cheville; ; articulation talo-crurale; ; left lobe of liver; ; utérus; ; parotide; ; tissu adipeux blanc; ; strie vasculaire; ; corpuscule carotidien; ; lobe pulmonaire droit; ; nerf optique;
	Plus de données d'expression de référence
	; ;
	Plus de données d'expression de référence
Gene Ontology
Fonction moléculaire	lipoteichoic acid binding; liaison protéique; liaison lipidique; signaling receptor binding; lipopolysaccharide binding; lipopeptide binding;
Composant cellulaire	membrane; exosome; région extracellulaire; surface cellulaire; milieu extracellulaire;
Processus biologique	detection of molecule of bacterial origin; lipid transport; toll-like receptor 4 signaling pathway; processus du système immunitaire; leukocyte chemotaxis involved in inflammatory response; cellular defense response; cellular response to lipoteichoic acid; defense response to bacterium; lipopolysaccharide transport; positive regulation of interleukin-8 production; positive regulation of interleukin-6 production; positive regulation of neutrophil chemotaxis; positive regulation of toll-like receptor 4 signaling pathway; positive regulation of chemokine production; negative regulation of tumor necrosis factor production; lipopolysaccharide-mediated signaling pathway; opsonisation; defense response to Gram-negative bacterium; positive regulation of tumor necrosis factor production; response to lipopolysaccharide; macrophage activation involved in immune response; positive regulation of respiratory burst involved in inflammatory response; acute-phase response; système immunitaire inné; defense response to Gram-positive bacterium; cellular response to lipopolysaccharide; positive regulation of macrophage activation; toll-like receptor signaling pathway; macromolecule localization; positive regulation of cytolysis; transport; cytokine-mediated signaling pathway;
	Sources:Amigo / QuickGO
Orthologues
	3929
	16803
	ENSG00000129988
	ENSMUSG00000016024
	P18428
	Q61805
	NM_004139
	NM_008489
	NP_004130
	NP_032515
	Wikidata
Voir/Editer Humain	Voir/Editer Souris

La protéine de liaison au lipopolysaccharide (ou Lipopolysaccharide Binding Protein) est une protéine qui, chez l’homme, est codée par le gène LBP^[5] situé sur le chromosome 20 humain.

La LBP est une protéine soluble de phase aiguë qui se lie au lipopolysaccharide bactérien (ou LPS) pour induire des réponses immunitaires en présentant le LPS à d'importants récepteurs de reconnaissance du motif de la surface cellulaire appelés CD14 et TLR4^[6]. Modèle:PBB Summary

La protéine codée par ce gène est impliquée dans la réponse immunologique en phase aiguë aux infections bactériennes à Gram négatif. Les bactéries à Gram négatif contiennent un glycolipide, un lipopolysaccharide (LPS), sur leur paroi cellulaire externe. Avec la protéine augmentant la perméabilité bactéricide (BPI ou batericidal permeability-increasing protein), la protéine codée se lie au LPS et interagit avec le récepteur CD14, jouant probablement un rôle dans la régulation des réponses des monocytes dépendant du LPS. Des études chez la souris suggèrent que la protéine codée est nécessaire à la réponse rapide du LPS en phase aiguë, mais pas à la clairance du LPS de la circulation. Cette protéine fait partie d'une famille de protéines structurellement et fonctionnellement liées, notamment la BPI, la protéine de transfert de cholestérol ester plasmatique (CETP) et la protéine de transfert de phospholipides (PLTP). Enfin, ce gène se trouve sur le chromosome 20, immédiatement en aval du gène BPI.

Interactions[modifier | modifier le code]

Il a été démontré que la protéine liant les lipopolysaccharides interagissait avec CD14,TLR2, TLR4 et le co-récepteur MD-2^[7]^,^[8]^,^[9].

Notes et références[modifier | modifier le code]

↑ ^{a b et c} GRCh38: Ensembl release 89: ENSG00000129988 - Ensembl, May 2017
↑ ^{a b et c} GRCm38: Ensembl release 89: ENSMUSG00000016024 - Ensembl, May 2017
↑ « Publications PubMed pour l'Homme », sur National Center for Biotechnology Information, U.S. National Library of Medicine
↑ « Publications PubMed pour la Souris », sur National Center for Biotechnology Information, U.S. National Library of Medicine
↑ « The genes for the lipopolysaccharide binding protein (LBP) and the bactericidal permeability increasing protein (BPI) are encoded in the same region of human chromosome 20 », Genomics, vol. 15, n^o 1,‎ mars 1993, p. 188–90 (PMID 8432532, DOI 10.1006/geno.1993.1030)
↑ « Essential roles of CD14 and lipopolysaccharide-binding protein for activation of toll-like receptor (TLR)2 as well as TLR4 Reconstitution of TLR2- and TLR4-activation by distinguishable ligands in LPS preparations », Eur. J. Biochem., vol. 268, n^o 16,‎ 2001, p. 4580–9 (PMID 11502220, DOI 10.1046/j.1432-1327.2001.02385.x)
↑ Thomas, Kapoor Mili, Sharma Shilpi et Bausinger Huguette, « Evidence of a trimolecular complex involving LPS, LPS binding protein and soluble CD14 as an effector of LPS response », FEBS Lett., Netherlands, vol. 531, n^o 2,‎ novembre 2002, p. 184–8 (ISSN 0014-5793, PMID 12417309, DOI 10.1016/S0014-5793(02)03499-3)
↑ Yu et Wright S D, « LPS-dependent interaction of Mac-2-binding protein with immobilized CD14 », J. Inflamm., UNITED STATES, vol. 45, n^o 2,‎ 1995, p. 115–25 (ISSN 1078-7852, PMID 7583357)
↑ Erridge, Pridmore, Eley et Stewart, « Lipopolysaccharides of Bacteroides fragilis, Chlamydia trachomatis and Pseudomonas aeruginosa signal via toll-like receptor 2. », Journal of Medical Microbiology, vol. 53, n^o Pt 8,‎ 2004, p. 735–40 (PMID 15272059, DOI 10.1099/jmm.0.45598-0)

Bibliographie[modifier | modifier le code]

RR. Schumann, SR. Leong, GW. Flaggs et al., Structure and function of lipopolysaccharide binding protein in Science 249 (4975), 1990 : 1429–31.
CG. Wilde, J.J. Seilhamer, M. McGrogan et al., Bactericidal/permeability-increasing protein and lipopolysaccharide (LPS)-binding protein. LPS binding properties and effects on LPS-mediated cell activation, in J. Biol. Chem. 269 (26), 1994 : 17411–17416. PMID 7517398.
CT. Park, SD. Wright, Plasma lipopolysaccharide-binding protein is found associated with a particle containing apolipoprotein A-I, phospholipid, and factor H-related proteins in J. Biol. Chem. 271 (30), 1996. PMID 8663389.
A. Nanbo, H. Nishimura, S. Nagasawa, Lipopolysaccharide binding protein from normal human plasma purified with high efficiency in Protein Expr. Purif. 10 (1), 1997 : 55–60. PMID 9179291.
J.A. Hubacek, C. Büchler, C. Aslanidis, G. Schmitz, The genomic organization of the genes for human lipopolysaccharide binding protein (LBP) and bactericidal permeability increasing protein (BPI) is highly conserved in Biochem. Biophys. Res. Commun. 236 (2), 1997 : 427–430. PMID 9240454.
RS. Jack, X. Fan, M. Bernheiden et al., Lipopolysaccharide-binding protein is required to combat a murine gram-negative bacterial infection in Nature 389 (6652), 1997 : 742–745. PMID 9338787.
CJ. Kirschning, J. Au-Young, N. Lamping et al., Similar organization of the lipopolysaccharide-binding protein (LBP) and phospholipid transfer protein (PLTP) genes suggests a common gene family of lipid-binding proteins in Genomics 46 (3), 1998 : 416–25. PMID 9441745.
L.J. Beamer, SF. Carroll, D. Eisenberg, The BPI/LBP family of proteins: a structural analysis of conserved regions in Protein Sci. 7 (4), 1998 : 906–914. PMID 9568897.
M. Sato, Y. Saeki, K. Tanaka, Y. Kaneda, Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system, in Biochem. Biophys. Res. Commun. 256 (2), 1999 : 385–390. PMID 10079194.
AC. Vreugdenhil, MA. Dentener, AM. Snoek et al., Lipopolysaccharide binding protein and serum amyloid A secretion by human intestinal epithelial cells during the acute phase response in Journal of Immunology 163 (5), 1999 : 2792–2798. PMID 10453023.
C.J. Vesy, R. L. Kitchens, G. Wolfbauer et al., Lipopolysaccharide-Binding Protein and Phospholipid Transfer Protein Release Lipopolysaccharides from Gram-Negative Bacterial Membranes, in Infect. Immun. 68 (5), 2000 : 2410–2417. PMID 10768924.
M.O. Labéta, K. Vidal, JE. Nores et al., Innate Recognition of Bacteria in Human Milk Is Mediated by a Milk-Derived Highly Expressed Pattern Recognition Receptor, Soluble Cd14 in J. Exp. Med. 191 (10), 2000 : 1807–1812. PMID 10811873.
M.A. Dentener, A. C. Vreugdenhil, P.H. Hoet et al., Production of the acute-phase protein lipopolysaccharide-binding protein by respiratory type II epithelial cells: implications for local defense to bacterial endotoxins in Am. J. Respir. Cell Mol. Biol. 23 (2), 2000 : 146–153. PMID 10919979.
I. Nagaoka, S. Hirota, F. Niyonsaba et al., Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells in Journal of Immunology 167 (6), 2001 : 3329–3338. PMID 11544322.
T. Gutsmann, M. Müller, SF. Carroll et al., Dual Role of Lipopolysaccharide (LPS)-Binding Protein in Neutralization of LPS and Enhancement of LPS-Induced Activation of Mononuclear Cells in Infect. Immun. 69 (11), 2001 : 6942–6950. PMID 11598069.
N. Iovine, J. Eastvold, P. Elsbach et al., The carboxyl-terminal domain of closely related endotoxin-binding proteins determines the target of protein-lipopolysaccharide complexes in J. Biol. Chem. 277 (10), 2002 : 7970–7978. PMID 11773072.
P. Deloukas, L. H. Matthews, J. Ashurst et al., The DNA sequence and comparative analysis of human chromosome 20 in Nature 414 (6866), 2002 : 865–871. PMID 11780052.
J. Kaden, P. Zwerenz, HG. Lambrecht, R. Dostatni, Lipopolysaccharide-binding protein as a new and reliable infection marker after kidney transplantation in Transpl. Int. 15 (4), 2002 : 163–172. PMID 11976738.
O. Reyes, MG. Vallespi, HE. Garay et al., Identification of single amino acid residues essential for the binding of lipopolysaccharide (LPS) to LPS binding protein (LBP) residues 86-99 by using an Ala-scanning library in J. Pept. Sci. 8 (4), 2002 : 144–150. PMID 11991204.

Liens externes[modifier | modifier le code]

Ressources relatives à la santé :
- Héritage mendélien chez l'humain
- Héritage mendélien chez l'humain
(en) MeSH lipopolysaccharide-binding+protein

Cet article incorpore le texte de la National Library of Medicine des États-Unis , qui est du domaine public .

[refGRCh38Ensembl-1] {a b et c} GRCh38: Ensembl release 89: ENSG00000129988 - Ensembl, May 2017

[refGRCm38Ensembl-2] {a b et c} GRCm38: Ensembl release 89: ENSMUSG00000016024 - Ensembl, May 2017

[3] « Publications PubMed pour l'Homme », sur National Center for Biotechnology Information, U.S. National Library of Medicine

[4] « Publications PubMed pour la Souris », sur National Center for Biotechnology Information, U.S. National Library of Medicine

[pmid8432532-5] « The genes for the lipopolysaccharide binding protein (LBP) and the bactericidal permeability increasing protein (BPI) are encoded in the same region of human chromosome 20 », Genomics, vol. 15, n^o 1,‎ mars 1993, p. 188–90 (PMID 8432532, DOI 10.1006/geno.1993.1030)

[6] « Essential roles of CD14 and lipopolysaccharide-binding protein for activation of toll-like receptor (TLR)2 as well as TLR4 Reconstitution of TLR2- and TLR4-activation by distinguishable ligands in LPS preparations », Eur. J. Biochem., vol. 268, n^o 16,‎ 2001, p. 4580–9 (PMID 11502220, DOI 10.1046/j.1432-1327.2001.02385.x)

[pmid12417309-7] Thomas, Kapoor Mili, Sharma Shilpi et Bausinger Huguette, « Evidence of a trimolecular complex involving LPS, LPS binding protein and soluble CD14 as an effector of LPS response », FEBS Lett., Netherlands, vol. 531, n^o 2,‎ novembre 2002, p. 184–8 (ISSN 0014-5793, PMID 12417309, DOI 10.1016/S0014-5793(02)03499-3)

[pmid7583357-8] Yu et Wright S D, « LPS-dependent interaction of Mac-2-binding protein with immobilized CD14 », J. Inflamm., UNITED STATES, vol. 45, n^o 2,‎ 1995, p. 115–25 (ISSN 1078-7852, PMID 7583357)

[pmid15272059-9] Erridge, Pridmore, Eley et Stewart, « Lipopolysaccharides of Bacteroides fragilis, Chlamydia trachomatis and Pseudomonas aeruginosa signal via toll-like receptor 2. », Journal of Medical Microbiology, vol. 53, n^o Pt 8,‎ 2004, p. 735–40 (PMID 15272059, DOI 10.1099/jmm.0.45598-0)

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