Old and new findings on lipopolysaccharide-binding protein: a soluble pattern-recognition molecule

被引:118
作者
Schumann, Ralf R. [1 ]
机构
[1] Charite, Inst Microbiol, Berlin, Germany
关键词
acute-phase protein; endotoxin recognition; innate immunity; lipopolysaccharide-binding protein (LBP); single-nucleotide polymorphism (SNP); BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN; GRAM-NEGATIVE BACTERIA; PHOSPHOLIPID TRANSFER PROTEIN; INNATE IMMUNE-RESPONSES; ACUTE PHASE REACTANT; TOLL-LIKE RECEPTORS; (LPS)-BINDING PROTEIN; SEPTIC SHOCK; PLUNC GENE; EPITHELIAL-CELLS;
D O I
10.1042/BST0390989
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
LBP [LPS (lipopolysaccharide)-binding protein] was discovered approximately 25 years ago. Since then, substantial progress has been made towards our understanding of its function in health and disease. Furthermore, the discovery of a large protein family sharing functional and structural attributes has helped in our knowledge. Still, key questions are unresolved, and here an overview on the old and new findings on LBP is given. LBP is an acute-phase protein of the liver, but is also synthesized in other cells of the organism. While LBP is named after the ability to bind to LPS of Gram-negative bacteria, it also can recognize other bacterial compounds, such as lipopeptides. It has been shown that LBP is needed to combat infections; however, the main mechanism of action is still not clear. New findings on natural genetic variations of LBP leading to functional consequences may help in further elucidating the mechanism of LBP and its role in innate immunity and disease.
引用
收藏
页码:989 / 993
页数:5
相关论文
共 90 条
[1]   Genetic variation of PLTP modulates lipoprotein profiles in hypoalphalipoproteinemia [J].
Aouizerat, BE ;
Engler, MB ;
Natanzon, Y ;
Kulkarni, M ;
Song, J ;
Eng, C ;
Huuskonen, J ;
Rivera, C ;
Poon, A ;
Bensley, M ;
Sehnert, A ;
Zellner, C ;
Malloy, M ;
Kane, J ;
Pullinger, CR .
JOURNAL OF LIPID RESEARCH, 2006, 47 (04) :787-793
[2]  
Beamer LJ, 1998, PROTEIN SCI, V7, P906
[3]   Structure of human BPI (bactericidal/permeability-increasing protein) and implications for related proteins [J].
Beamer, LJ .
BIOCHEMICAL SOCIETY TRANSACTIONS, 2003, 31 :791-794
[4]   Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution [J].
Beamer, LJ ;
Carroll, SF ;
Eisenberg, D .
SCIENCE, 1997, 276 (5320) :1861-1864
[5]   Characterisation of the human plunc gene, a gene product with an upper airways and nasopharyngeal restricted expression pattern [J].
Bingle, CD ;
Bingle, L .
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 2000, 1493 (03) :363-367
[6]   Meet the relatives: a family of BPI- and LBP-related proteins [J].
Bingle, CD ;
Craven, CJ .
TRENDS IN IMMUNOLOGY, 2004, 25 (02) :53-55
[7]   Phylogenetic and evolutionary analysis of the PLUNC gene family [J].
Bingle, CD ;
Leclair, EE ;
Havard, S ;
Bingle, L ;
Gillingham, P ;
Craven, CJ .
PROTEIN SCIENCE, 2004, 13 (02) :422-430
[8]   PLUNC: A novel family of candidate host defence proteins expressed in the upper airways and nasopharynx [J].
Bingle, CD ;
Craven, CJ .
HUMAN MOLECULAR GENETICS, 2002, 11 (08) :937-943
[9]   CETP gene variation: relation to lipid parameters and cardiovascular risk [J].
Boekholdt, SM ;
Kuivenhoven, JA ;
Hovingh, GK ;
Jukema, JW ;
Kastelein, JJP ;
van Tol, A .
CURRENT OPINION IN LIPIDOLOGY, 2004, 15 (04) :393-398
[10]   LPS-binding protein-deficient mice have an impaired defense against Gram-negative but not Gram-positive pneumonia [J].
Branger, J ;
Florquin, S ;
Knapp, S ;
Leemans, JC ;
Pater, JM ;
Speelman, P ;
Golenbock, DT ;
van der Poll, T .
INTERNATIONAL IMMUNOLOGY, 2004, 16 (11) :1605-1611