Tobias P S, Mathison J C, Ulevitch R J
Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.
J Biol Chem. 1988 Sep 25;263(27):13479-81.
The lipopolysaccharides (LPS) of Gram-negative bacteria initiate potentially fatal processes in many host organisms. Recently published amino acid sequence data suggest that there is a family of LPS binding proteins that may participate in the host response to Gram-negative bacteremia. The first two members of the family to be identified are an LPS binding protein present in serum after an acute phase response in humans, mice, rabbits, and rats and a bactericidal/permeability increasing protein present in the primary granules of human and rabbit neutrophils. LPS binding protein and bactericidal/permeability increasing protein share an ability to bind to LPS, have homologous NH2-terminal amino acid sequences, and are immunologically cross-reactive. Nevertheless, these two molecules differ in their effects on LPS and Gram-negative bacteria, in their sites of biosynthesis, and localization in vivo.
革兰氏阴性菌的脂多糖（LPS）在许多宿主生物体中引发潜在的致命过程。最近公布的氨基酸序列数据表明，存在一个LPS结合蛋白家族，它们可能参与宿主对革兰氏阴性菌血症的反应。该家族最早被鉴定的两个成员是在人类、小鼠、兔子和大鼠急性期反应后血清中存在的一种LPS结合蛋白，以及人类和兔子中性粒细胞初级颗粒中存在的一种杀菌/通透性增加蛋白。LPS结合蛋白和杀菌/通透性增加蛋白都具有结合LPS的能力，具有同源的NH2末端氨基酸序列，并且在免疫上具有交叉反应性。然而，这两种分子在对LPS和革兰氏阴性菌的作用、生物合成位点以及体内定位方面存在差异。
