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LBP
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4M4D
Identifiers
Aliases	LBP, BPIFD2, lipopolysaccharide binding protein
External IDs	OMIM: 151990; MGI: 1098776; HomoloGene: 3055; GeneCards: LBP; OMA:LBP - orthologs
Gene location (Human)
Chr.	Chromosome 20 (human)
End	38,377,013 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	158,174,772 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; testicle; ; tibialis anterior muscle; ; gastrocnemius muscle; ; muscle of thigh; ; appendix; ; deltoid muscle; ; subcutaneous adipose tissue; ; glutes; ; right lobe of thyroid gland;
	Top expressed in
	gastrula; ; choroid plexus of fourth ventricle; ; decidua; ; Epithelium of choroid plexus; ; lumbar spinal ganglion; ; ankle; ; ankle joint; ; stroma of bone marrow; ; left lobe of liver; ; uterus;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	lipoteichoic acid binding; protein binding; lipid binding; signaling receptor binding; lipopolysaccharide binding; lipopeptide binding;
Cellular component	membrane; extracellular exosome; extracellular region; cell surface; extracellular space;
Biological process	detection of molecule of bacterial origin; lipid transport; toll-like receptor 4 signaling pathway; immune system process; 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; opsonization; 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; innate immune response; 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
Orthologs
	3929
	16803
	ENSG00000129988
	ENSMUSG00000016024
	P18428
	Q61805
	NM_004139
	NM_008489
	NP_004130
	NP_032515
	Wikidata
View/Edit Human	View/Edit Mouse

Lipopolysaccharide binding protein (LBP) is a protein that in humans is encoded by the LBP gene.^[5]^[6]

LBP is a soluble acute-phase protein that binds to bacterial lipopolysaccharide (or LPS) to elicit immune responses by presenting the LPS to important cell surface pattern recognition receptors called CD14 and TLR4.^[7]

The protein encoded by this gene is involved in the acute-phase immunologic response to gram-negative bacterial infections. Gram-negative bacteria contain a glycolipid, lipopolysaccharide (LPS), on their outer cell wall. Together with bactericidal permeability-increasing protein (BPI), the encoded protein binds LPS and interacts with the CD14 receptor, probably playing a role in regulating LPS-dependent monocyte responses. Studies in mice suggest that the encoded protein is necessary for the rapid acute-phase response to LPS but not for the clearance of LPS from circulation. This protein is part of a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). Finally, this gene is found on chromosome 20, immediately downstream of the BPI gene.^[6]

Clinical significance

LPS exposure induces LBP production.^[8] LBP is synthesized by the liver, adipose tissue, and intestinal cells.^[8] Dietary glucose and saturated fats acutely increase plasma LBP.^[8]

The proinflammatory activity of plasma LPS is increased by LBP, which is higher in obesity.^[9]

Plasma LBP is used as a better biomarker of plasma LPS than LPS itself due to the short half-life of LPS.^[8]

Interactions

Lipopolysaccharide-binding protein has been shown to interact with CD14, TLR2, TLR4 and the co-receptor MD-2.^[10]^[11]^[12]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000129988 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000016024 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Gray PW, Corcorran AE, Eddy RL Jr, Byers MG, Shows TB (March 1993). "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. 15 (1): 188–90. doi:10.1006/geno.1993.1030. PMID 8432532.
^ ^a ^b "Entrez Gene: LBP lipopolysaccharide binding protein".
^ Muta T, Takeshige K (2001). "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. 268 (16): 4580–9. doi:10.1046/j.1432-1327.2001.02385.x. PMID 11502220.
^ ^a ^b ^c ^d Djuric Z (2017). "Obesity-associated cancer risk: the role of intestinal microbiota in the etiology of the host proinflammatory state". Translational Research. 179: 155–167. doi:10.1016/j.trsl.2016.07.017. PMC 5164980. PMID 27522986.
^ Tuomi K, Logomarsino JV (2016). "Bacterial Lipopolysaccharide, Lipopolysaccharide-Binding Protein, and Other Inflammatory Markers in Obesity and After Bariatric Surgery". Metabolic Syndrome and Related Disorders. 14 (6): 279–288. doi:10.1089/met.2015.0170. PMID 27228236.
^ Thomas CJ, Kapoor Mili, Sharma Shilpi, Bausinger Huguette, Zyilan Umit, Lipsker Dan, Hanau Daniel, Surolia Avadhesha (November 2002). "Evidence of a trimolecular complex involving LPS, LPS binding protein and soluble CD14 as an effector of LPS response". FEBS Lett. 531 (2): 184–8. doi:10.1016/S0014-5793(02)03499-3. ISSN 0014-5793. PMID 12417309. S2CID 25135963.
^ Yu B, Wright S D (1995). "LPS-dependent interaction of Mac-2-binding protein with immobilized CD14". J. Inflamm. 45 (2): 115–25. ISSN 1078-7852. PMID 7583357.
^ Erridge C, Pridmore A, Eley A, Stewart J, Poxton IR (2004). "Lipopolysaccharides of Bacteroides fragilis, Chlamydia trachomatis and Pseudomonas aeruginosa signal via toll-like receptor 2". Journal of Medical Microbiology. 53 (Pt 8): 735–40. doi:10.1099/jmm.0.45598-0. PMID 15272059.