BioPAX pathway converted from "Association of LBP with LPS" in the Reactome database.Association of LBP with LPS

Association of LBP with LPS

Lipopolysaccharide-binding protein (LBP) is a ~60-kDa serum glycoprotein which transfers LPS to both membrane-bound and soluble CD14. The LPS binding site of LBP consists of basic residues that bind the phosphorylated head of the bacterial lipid A. <p>LBP is an acute-phase opsonin that binds gram-negative bacteria and bacterial fragments and promote the interaction of coated bacteria with phagocytes.

Authored: de Bono, B, 2005-08-16 10:54:15Reviewed: Gay, NJ, 2006-04-24 16:48:17Reviewed: Gillespie, ME, 2010-11-30Reviewed: Granucci, Francesca, Zanoni, Ivan, 2012-11-13Edited: Shamovsky, V, 2010-11-16

Reactome DB_ID: 166005

extracellular regionGO0005576

lipopolysaccharide [ChEBI:16412]

lipopolysaccharide

lipopolysaccharidesLPS

Reactomehttp://www.reactome.orgChEBI16412

Reactome DB_ID: 166010

UniProt:P18428 LBP

LBP

LBPFUNCTION Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria (PubMed:7517398, PubMed:24120359). Acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide (PubMed:7517398, PubMed:24120359).SUBUNIT When bound to LPS, interacts (via C-terminus) with soluble and membrane-bound CD14.TISSUE SPECIFICITY Detected in blood serum (at protein level).SIMILARITY Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

Homo sapiens

NCBI Taxonomy9606UniProtP18428

Chain Coordinates

EQUAL

481

EQUAL

Reactome DB_ID: 166013

LBP:bacterial LPS [extracellular region]

LBP:bacterial LPS

Reactome DB_ID: 166005

Reactome DB_ID: 166010

EQUAL

481

EQUAL

Reactome Database ID Release 75166013Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=166013ReactomeR-HSA-166013

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-166013.1Reactome Database ID Release 75166015Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=166015ReactomeR-HSA-166015

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-166015.32477488Pubmed1989Lipopolysaccharide (LPS) binding protein opsonizes LPS-bearing particlesWright, SDTobias, PSUlevitch, RJRamos, RAJ Exp Med 170:1231-411698311Pubmed1990CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding proteinWright, SDRamos, RATobias, PSUlevitch, RJMathison, JCScience 249:1431-319269309Pubmed2009Cationic lipids activate cellular cascades. Which receptors are involved?Lonez, CLensink, MFVandenbranden, MRuysschaert, JMBiochim Biophys Acta 1790:425-30

INHIBITION

Reactome Database ID Release 756810041Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6810041ReactomeR-HSA-6810041

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-6810041.1

Reactome DB_ID: 6806211

UniProt:P17213 BPI

BPI

BPIFUNCTION The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.SUBUNIT Monomer. Homodimer; disulfide-linked.TISSUE SPECIFICITY Restricted to cells of the myeloid series.DOMAIN The N-terminal region may be exposed to the interior of the granule, whereas the C-terminal portion may be embedded in the membrane. During phagocytosis and degranulation, proteases may be released and activated and cleave BPI at the junction of the N- and C-terminal portions of the molecule, providing controlled release of the N-terminal antibacterial fragment when bacteria are ingested.DOMAIN The N- and C-terminal barrels adopt an identical fold despite having only 13% of conserved residues.SIMILARITY Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.

UniProtP17213

EQUAL

487

EQUAL