CD66 receptor specificity exhibited by neisserial Opa variants controlled by protein determinants in CD66 N-domains
CD66 receptor specificity exhibited by neisserial Opa variants controlled by protein determinants in CD66 N-domains
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DOI：
10.1073/pnas.95.16.9584
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发表时间：
1998-08-04
影响因子：
11.1
通讯作者：
Belland, RJ
中科院分区：
文献类型：
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作者：
Bos, MP;Kuroki, M;Belland, RJ
淋病奈瑟菌菌株MS 11能够在其外表面上表达11种不同的不透明（Opa）蛋白。许多这些Opa蛋白已显示通过结合存在于人细胞上的CD 66受体作为粘附素起作用。CD 66抗原或癌胚抗原家族成员构成属于免疫球蛋白超家族的糖蛋白家族。Opa变体以不同的方式识别这类受体，使得某些Opa变体识别多达四种不同的CD 66受体（CD 66 a、-c、-d和-e），而其他变体仅识别两种（CD 66 a和-e）或不识别。本研究探讨了这种受体向性的基础。我们的数据表明，糖型的CD 66 e和去糖基化的CD 66 e被淋球菌识别的Opa特异性的方式。大肠杆菌中表达的CD 66受体的重组N-末端结构域的Opa变体的结合反映了Opa变体对表达天然CD 66分子的HeLa细胞的粘附特异性。这些数据表明Opa变体对CD 66受体的识别是由CD 66 N结构域的蛋白质骨架介导的。此外，通过使用不同CD 66 N-结构域之间的嵌合构建体，我鉴定了CD 66 e N-结构域上特定Opa变体组的不同结合区域，表明Opa变体对CD 66受体的差异识别由受体N-结构域上特异性结合区域的存在决定。
Neisseria gonorrhoeae strain MS11 is able to express 11 different opacity (Opa) proteins on its outer surface. A number of these Opa proteins have been shown to function as adhesins through binding of CD66 receptors present on human cells. CD66 antigens, or carcinoembryonic antigen family members, constitute a family of glycoproteins belonging to the immunoglobulin superfamily. Opa variants recognize this class of receptors in a differential manner such that certain Opa variants recognize up to four different CD66 receptors (CD66a, -c, -d, and -e), whereas others recognize only two (CD66a and -e) or none. Ve explored the basis for this receptor tropism in the present study. Our data show that glycoforms of CD66e and deglycosylated CD66e are recognized by gonococci in an Opa-specific manner. Binding by Opa variants of recombinant N-terminal domains of CD66 receptors expressed in Escherichia coli reflected the adherence specificities of Opa variants to HeLa cells expressing native CD66 molecules. These data indicate that recognition of CD66 receptors by Opa variants is mediated by the protein backbone of the CD66 N-domains. Furthermore, by using chimeric constructs between different CD66 N-domains me identified distinct binding regions on the CD66e N-domain for specific groups of Opa variants, suggesting that the differential recognition of CD66 receptors by Opa variants is dictated by the presence of specific binding regions on the N-domain of the receptor.