Pils Stefan, Gerrard Dave T, Meyer Axel, Hauck Christof R
Lehrstuhl Zellbiologie, Fachbereich Biologie X908, Universität Konstanz, Universitätsstrasse 10, 78457 Konstanz, Germany.
Int J Med Microbiol. 2008 Oct;298(7-8):553-60. doi: 10.1016/j.ijmm.2008.04.005. Epub 2008 Jul 7.
Carcinoembryonic antigen-related cell adhesion molecule 3 (CEACAM3) is an immunoglobulin-related glycoprotein exclusively expressed on granulocytes. In contrast to other members of the CEACAM family, CEACAM3 does not support cell-cell adhesion, but rather mediates the opsonin-independent recognition and elimination of a restricted set of human-specific Gram-negative bacterial pathogens including Neisseria gonorrhoeae, Haemophilus influenzae, and Moraxella catarrhalis. Within the last 4 years, molecular determinants of CEACAM3 function and CEACAM3-initiated signaling pathways have been elucidated. Sequence comparison between CEACAM3 and other CEACAM family members points to a chimeric origin of this receptor with the bacteria-binding extracellular domain and the function-promoting intracellular domain derived from different genes. This review summarizes the current knowledge about the structure-function relationship of CEACAM3 and tries to combine these molecular aspects with a plausible scenario concerning the evolutionary origin of this phagocyte receptor in the light of host-pathogen adaptation.
癌胚抗原相关细胞黏附分子3（CEACAM3）是一种仅在粒细胞上表达的免疫球蛋白相关糖蛋白。与CEACAM家族的其他成员不同，CEACAM3不支持细胞间黏附，而是介导对包括淋病奈瑟菌、流感嗜血杆菌和卡他莫拉菌在内的一组有限的人类特异性革兰氏阴性细菌病原体的不依赖调理素的识别和清除。在过去4年中，CEACAM3功能的分子决定因素和CEACAM3启动的信号通路已得到阐明。CEACAM3与其他CEACAM家族成员之间的序列比较表明，该受体具有嵌合起源，其细菌结合细胞外结构域和功能促进细胞内结构域源自不同基因。本综述总结了目前关于CEACAM3结构-功能关系的知识，并试图根据宿主-病原体适应性，将这些分子方面与关于这种吞噬细胞受体进化起源的合理设想相结合。
