HUMAN CD4 BINDS IMMUNOGLOBULINS

被引：52
作者：
LENERT, P
KROON, D
SPIEGELBERG, H
GOLUB, ES
ZANETTI, M
机构：
[1] UNIV CALIF SAN DIEGO,DEPT MED,DIV DERMATOL,SAN DIEGO,CA 92103
[2] RW JOHNSON PHARMACEUT RES INST,RARITAN,NJ 08869
[3] SCRIPPS CLIN & RES FDN,RES INST,DEPT IMMUNOL,LA JOLLA,CA 92037
[4] SCRIPPS CLIN & RES FDN,RES INST,JOHNSON & JOHNSON LABS,LA JOLLA,CA 92037
来源：
SCIENCE | 1990年 / 248卷 / 4963期
关键词：
D O I：
10.1126/science.2363051
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
T cell glycoprotein CD4 binds to class II major histocompatibility molecules and to the human immunodeficiency virus (HIV) envelope protein gp120. Recombinant CD4 (rCD4) bound to polydonal immunoglobulin (Ig) and 39 of 50 (78%) human myeloma proteins. This binding depended on the Fab and not the Fc portion of Ig and was independent of the light chain. Soluble rCD4, HIV gp120, and sulfated dextrans inhibited the CD4-Ig interaction. With the use of a panel of synthetic peptides, the region critical for binding to Ig was localizd to amino acids 21 to 38 of the first extracellular domain of CD4. CD4-bound antibody (Ab) complexed with antigen approximately 100 times better than Ab alone. This activity may contribute to the Ab-mediated enhancement of cellular HIV interaction that appears to depend on a trimolecular complex of HIV, antibodies to gp120, and CD4.
引用
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页码：1639 / 1643
页数：5
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