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小鼠和人类重组脂多糖结合蛋白(LBP)在脂多糖和革兰氏阴性菌中的反应性。

Reactivity of murine and human recombinant LPS-binding protein (LBP) within LPS and gram negative bacteria.

作者信息

Lengacher S, Jongeneel C V, Le Roy D, Lee J D, Kravchenko V, Ulevitch R J, Glauser M P, Heumann D

机构信息

Division of Infectious Diseases, CHUV, Laussane, Switzerland.

出版信息

J Inflamm. 1995;47(4):165-72.

PMID:9144073
Abstract

The serum lipopolysaccharide (LPS) binding protein, LBP, has been shown to greatly enhance cellular responses to low concentrations of LPS. Purified LBP facilitates the transfer of LPS to membrane-bound or soluble CD14; the CD14/LPS complex then triggers a signal in responsive cells. We have cloned and sequenced a cDNA encoding murine LBP, and produced recombinant murine LBP using a baculovirus expression system. Using either a solid-phase or a cytofluorometric assay, recombinant murine and human LBP were found to bind avidly to free LPS, but only weakly to live bacteria from most LPS-containing Gram negative strains. Binding correlated loosely with the length and composition of the polysaccharide O chains. However, recombinant LBP did bind well to all heat-killed bacterial preparations. These findings suggest that LBP could be implicated in the response to killed but not live Gram negative bacteria.

摘要

血清脂多糖(LPS)结合蛋白LBP已被证明能极大地增强细胞对低浓度LPS的反应。纯化的LBP有助于将LPS转移至膜结合型或可溶性CD14;然后,CD14/LPS复合物在反应性细胞中触发信号。我们克隆并测序了编码小鼠LBP的cDNA,并使用杆状病毒表达系统制备了重组小鼠LBP。使用固相或细胞荧光测定法发现,重组小鼠和人LBP能与游离LPS紧密结合,但与大多数含LPS的革兰氏阴性菌株的活菌结合较弱。结合与多糖O链的长度和组成松散相关。然而,重组LBP确实能很好地结合所有热灭活细菌制剂。这些发现表明,LBP可能参与对热灭活革兰氏阴性菌而非活菌的反应。

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