Chiang Su-Chi, Chang Cheng-Chi, Lin Yi-Chun, Ng Hang-Pong, Lee Sho Tone
Division of Infectious Diseases and Immunology, Institute of Biomedical Sciences (IBMS), No. 128, Academia Road Section 2, Nankang, Taipei 11529, Taiwan, ROC.
Int J Parasitol. 2007 Jul;37(8-9):1001-11. doi: 10.1016/j.ijpara.2007.01.005. Epub 2007 Jan 19.
The binding of each intercellular adhesive molecule (ICAM) molecule fragment from Leishmania amazonensis (ICAM-L) to host macrophages was investigated using an indirect immunofluorescent sandwich technique, based on the observation that ICAM-L can block the uptake of L. amazonensis on the macrophage surface and all prepared ICAM-L fragments can react with rabbit anti-ICAM-L antiserum. The ICAM-L fragments lacking the loop 1 (LI) structure failed to bind to macrophages, and the disruption of the LI structure by mercaptoethanol led to the failure of binding. The fragments containing the LI structure functioned similarly to ICAM-L, by temporarily retarding host cell growth and cell cycle progression, and inhibiting the Leishmania infection of host macrophages. These results suggest that LI constitutes the main determinant of the ICAM-L molecule in binding to, and infection of, host macrophages.
基于亚马逊利什曼原虫的细胞间粘附分子（ICAM）分子片段（ICAM-L）能阻断巨噬细胞表面亚马逊利什曼原虫的摄取以及所有制备的ICAM-L片段都能与兔抗ICAM-L抗血清发生反应这一观察结果，采用间接免疫荧光夹心技术研究了ICAM-L与宿主巨噬细胞的结合情况。缺乏环1（L1）结构的ICAM-L片段无法与巨噬细胞结合，而巯基乙醇对L1结构的破坏导致结合失败。含有L1结构的片段的功能与ICAM-L相似，可暂时延缓宿主细胞生长和细胞周期进程，并抑制宿主巨噬细胞的利什曼原虫感染。这些结果表明，L1是ICAM-L分子与宿主巨噬细胞结合及感染的主要决定因素。
