生物
抗体
受体
病毒学
人巨细胞病毒
免疫球蛋白D
免疫球蛋白G
Fc受体
仓鼠
分子生物学
病毒
巨细胞病毒
单纯疱疹病毒
免疫球蛋白Fc片段
免疫学
疱疹病毒科
B细胞
生物化学
病毒性疾病
作者
Annika Antonsson,Peter Johansson
标识
DOI:10.1099/0022-1317-82-5-1137
摘要
Human cytomegalovirus (HCMV)-infected cells express a virus-encoded receptor that is able to bind the Fc part of IGG: Some basic binding properties of this Fc receptor (FcR) have been examined. The affinity constant (K(a)) for human IgG Fc fragment in its interaction with acetone-fixed, HCMV-infected human embryonic lung fibroblasts was estimated to be around 2 x 10(8) M(-1) and the number of binding sites was estimated to be around 2 x 10(6) per cell. Of the human IgG, IgA, IgM and IgD classes, only IgG reacted with the receptor, and all four of the IgG subclasses were reactive. IgG from rabbit, hamster, cat, swine and horse exhibited binding to the HCMV FcR, in contrast to IgG from mouse, rat, guinea pig, dog, sheep, goat, cow and chicken. Immunoglobulins with and without HCMV IgG FcR-binding properties, like IgG from rabbit and mouse, can be of value in revealing the functional importance of the receptor. When the immunoglobulins were tested against herpes simplex virus type 1-induced FcR, both similarities and differences in immunoreactivity were seen relative to the HCMV FcR, which makes it unlikely that the binding sites for these two herpesvirus FcRs on the IgG molecule are identical.
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