PROSITE documentation PDOC00367
LBP / BPI / CETP family signature


The following mammalian lipid-binding serum glycoproteins belong to the same family [1,2,3]:

  • Lipopolysaccharide-binding protein (LBP). LBP binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. The LBP/LPS complex seems to interact with the CD14 receptor and may be responsible for the secretion of α-TNF.
  • Bactericidal permeability-increasing protein (BPI). Like LBP, BPI binds LPS and has a cytotoxic activity on Gram-negative bacteria.
  • Cholesteryl ester transfer protein (CETP). CETP is involved in the transfer of insoluble cholesteryl esters in reverse cholesterol transport.
  • Phospholipid transfer protein (PLTP). May play a key role in extracellular phospholipid transport and modulation of HDL particles.

These proteins are structurally related and share many regions of sequence similarities. As a signature pattern we have selected one of these regions, which is located in the N-terminal section of these proteins; a region which could be involved in the binding to the lipids [2].

Expert(s) to contact by email:

Jongeneel C.V.

Last update:

December 2004 / Pattern and text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

LBP_BPI_CETP, PS00400; LBP / BPI / CETP family signature  (PATTERN)


1AuthorsSchumann R.R. Leong S.R. Flaggs G.W. Gray P.W. Wright S.D. Mathison J.C. Tobias P.S. Ulevitch R.J.
TitleStructure and function of lipopolysaccharide binding protein.
SourceScience 249:1429-1431(1990).
PubMed ID2402637

2AuthorsGray P.W. Flaggs G. Leong S.R. Gumina R.J. Weiss J. Ooi C.E. Elsbach P.
TitleCloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations.
SourceJ. Biol. Chem. 264:9505-9509(1989).
PubMed ID2722846

3AuthorsDay J.R. Albers J.J. Lofton-Day C.E. Gilbert T.L. Ching A.F.T. Grant F.J. O'Hara P.J. Marcovina S.M. Adolphson J.L.
TitleComplete cDNA encoding human phospholipid transfer protein from human endothelial cells.
SourceJ. Biol. Chem. 269:9388-9391(1994).
PubMed ID8132678

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