Functional comparison of the mouse DC-SIGN, SIGNR1, SIGNR3 and Langerin, C-type lectins.
Functional comparison of the mouse DC-SIGN, SIGNR1, SIGNR3 and Langerin, C-type lectins.
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DOI：
10.1093/intimm/dxh084
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发表时间：
2004-06
影响因子：
4.4
通讯作者：
K. Takahara;Yusuke Yashima;Y. Omatsu;H. Yoshida;Y. Kimura;Young‐Sun Kang;R. Steinman;Chae Gyu Park;K. Inaba
中科院分区：
文献类型：
--
作者：
K. Takahara;Yusuke Yashima;Y. Omatsu;H. Yoshida;Y. Kimura;Young‐Sun Kang;R. Steinman;Chae Gyu Park;K. Inaba
小鼠（m）DC-SIGN家族由位于8号染色体上紧邻的几种同源II型跨膜蛋白组成，并且具有单个羧基末端碳水化合物识别结构域。我们首先使用转染的非巨噬细胞系来比较这些凝集素中的三种-DC-SIGN、SIGNR 1和SIGNR 3-与另一种同源物mLangerin的多糖和微生物摄取能力。每个分子在其碳水化合物识别结构域中共享潜在的甘露糖识别EPN基序。使用抗Tag抗体跟踪Tag标记的转染子，我们发现每个分子都可以被内化，尽管速率不同。然而，mDC-SIGN不能摄取FITC-葡聚糖、FITC-卵清蛋白、酵母聚糖或热灭活的白色念珠菌。其他三种凝集素显示出不同的碳水化合物识别特性，通过在37 ℃下阻断FITC-葡聚糖摄取和在4 ℃下甘露聚糖结合活性来评估。此外，只有SIGNR 1是有效的介导的革兰氏阴性细菌，如大肠杆菌和鼠伤寒沙门氏菌的转染细胞的捕获，而没有测试的凝集素是有能力捕获革兰氏阳性细菌，金黄色葡萄球菌。有趣的是，缺乏胞质结构域的SIGNR 1的转染子能够以EDTA或甘露聚糖而不是海带多糖消除的方式结合FITC-酵母聚糖。此外，居民腹膜CD 11b+细胞表达SIGNR 1结合酵母聚糖在4摄氏度与海带多糖敏感受体。因此，这些同源C型凝集素具有不同的识别模式的微生物，尽管在碳水化合物识别域的相似性。
The mouse (m) DC-SIGN family consists of several homologous type II transmembrane proteins located in close proximity on chromosome 8 and having a single carboxyl terminal carbohydrate recognition domain. We first used transfected non-macrophage cell lines to compare the polysaccharide and microbial uptake capacities of three of these lectins--DC-SIGN, SIGNR1 and SIGNR3--to another homologue mLangerin. Each molecule shares a potential mannose-recognition EPN-motif in its carbohydrate recognition domain. Using an anti-Tag antibody to follow Tag-labeled transfectants, we found that each molecule could be internalized, although the rates differed. However, mDC-SIGN was unable to take up FITC-dextran, FITC-ovalbumin, zymosan or heat-killed Candida albicans. The other three lectins showed distinct carbohydrate recognition properties, assessed by blocking FITC-dextran uptake at 37 degrees C and by mannan binding activity at 4 degrees C. Furthermore, only SIGNR1 was efficient in mediating the capture by transfected cells of Gram-negative bacteria, such as Escherichia coli and Salmonella typhimurium, while none of the lectins tested were competent to capture Gram-positive bacteria, Staphylococcus aureus. Interestingly, transfectants with SIGNR1 lacking the cytoplasmic domain were capable of binding FITC-zymosan in a manner that was abolished by EDTA or mannan, but not laminarin. In addition, resident peritoneal CD11b+ cells expressing SIGNR1 bound zymosan at 4 degrees C in concert with a laminarin-sensitive receptor. Therefore these homologous C-type lectins have distinct recognition patters for microbes despite similarities in the carbohydrate recognition domains.