Immulectin‐4 from the tobacco hornworm Manduca sexta binds to lipopolysaccharide and lipoteichoic acid
Immulectin‐4 from the tobacco hornworm Manduca sexta binds to lipopolysaccharide and lipoteichoic acid
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DOI：
10.1111/j.1365-2583.2006.00618.x
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发表时间：
2006-04
影响因子：
2.6
通讯作者：
X-Q Yu;Erjun Ling;M. Tracy;Y. Zhu
中科院分区：
文献类型：
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作者：
X-Q Yu;Erjun Ling;M. Tracy;Y. Zhu
昆虫C型凝集素在先天免疫中作为模式识别受体发挥作用。在烟草天蛾Manduca sexta中，我们以前分离出三种C型凝集素，称为免疫凝集素，它们参与先天免疫反应。在这里，我们报告了immulectin家族的一个新成员，immulectin-4（IML-4）。在对照幼虫的脂肪体中检测到IML-4 mRNA，并且当幼虫注射细菌时，在脂肪体中诱导IML-4 mRNA。重组IML-4与细菌脂多糖（LPS）和脂磷壁酸（LTA）结合，并且结合活性不受添加钙或EGTA的影响。IML-4凝集细菌和酵母，IML-4对大肠杆菌的凝集具有浓度和钙依赖性。IML-4还增强了血细胞包裹和黑化。
Insect C‐type lectins function as pattern recognition receptors in innate immunity. In the tobacco hornworm Manduca sexta, we have previously isolated three C‐type lectins named immulectins, which are involved in innate immune responses. Here, we report a new member of the immulectin family, immulectin‐4 (IML‐4). IML‐4 mRNA was detected in the fat body of control larvae and was induced in the fat body when larvae were injected with bacteria. Recombinant IML‐4 bound to bacterial lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and the binding activity was not affected by addition of calcium or EGTA. IML‐4 agglutinated bacteria and yeast, and agglutination of Escherichia coli by IML‐4 was concentration‐ and calcium‐dependent. IML‐4 also enhanced haemocyte encapsulation and melanization.