Lipopolysaccharide (LPS)-binding proteins BPI and LBP form different types of complexes with LPS

被引:96
作者
Tobias, PS
Soldau, K
Iovine, NM
Elsbach, P
Weiss, J
机构
[1] NYU, SCH MED, DEPT MED, NEW YORK, NY 10016 USA
[2] NYU, SCH MED, DEPT MICROBIOL, NEW YORK, NY 10016 USA
关键词
D O I
10.1074/jbc.272.30.18682
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
Lipopolysaccharide (LPS)-binding protein (LBP) and bactericidal/permeability-increasing protein (BPI) are closely related LPS binding proteins whose binding to LPS has markedly different functional consequences, To gain better insight into the possible basis of these functional differences, the physical properties of LBP-LPS and BPI-LPS complexes have been compared in this study by sedimentation, light scattering, and fluorescence analyses, These studies reveal dramatic differences in the physical properties of LPS complexed to LBP versus BPI, They suggest that of the two proteins, only LBP can disperse LPS aggegates, However, BPI can enhance both the sedimentation velocity and apparent size of LPS aggregates while inhibiting LPS-LBP binding even at very low (1:40 to 1:20) BPI:LPS molar ratios.
引用
收藏
页码:18682 / 18685
页数:4
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