期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 6, 页码 3886-3896出版社
ELSEVIER
DOI: 10.1074/jbc.M112.415679
关键词
-
资金
- Agriculture and Food Research Initiative [2008-35204-04626, 2009-65119-05993, 2008-55620-18710, 4535-CU-USDA-8710, 3954-CU-USDA-8710]
- Animal Formula Fund [NY-478455, NY-478437]
- Biotechnology Research and Development Corp.
The antigen 85 complex (Ag85) consists of three predominantly secreted proteins (Ag85A, Ag85B, and Ag85C), which play a key role in the mycobacterial pathogenesis and also possess enzymatic mycolyltransferase activity involved in cell wall synthesis. Ag85 is not only considered to be a virulence factor because its expression is essential for intracellular survival within macrophages, but also because it contributes to adherence, invasion, and dissemination of mycobacteria in host cells. In this study, we report that the extracellular matrix components, elastin and its precursor (tropoelastin) derived from human aorta, lung, and skin, serve as binding partners of Ag85 from Mycobacterium tuberculosis. The binding affinity of M. tuberculosis Ag85 to human tropoelastin was characterized (K-D = 0.13 +/- 0.006 mu M), and a novel Ag85-binding motif, AAA-KAA(K/Q)(Y/F), on multiple tropoelastin modules was identified. In addition, the negatively charged Glu-258 of Ag85 was demonstrated to participate in an electrostatic interaction with human tropoelastin. Moreover, binding of Ag85 on elastin siRNA-transfected Caco-2 cells was significantly reduced (34.3%), implying that elastin acts as an important ligand contributing to mycobacterial invasion.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据