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Science 29 June 1990:
Vol. 248. no. 4963, pp. 1639 - 1643
DOI: 10.1126/science.2363051
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Articles

Science, Vol 248, Issue 4963, 1639-1643
Copyright © 1990 by American Association for the Advancement of Science

articles

Human CD4 binds immunoglobulins

P Lenert, D Kroon, H Spiegelberg, ES Golub, and M Zanetti

Department of Medicine, University of California, San Diego 92103.

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 polyclonal 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 localized 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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Characterization of Superantigen-Induced Clonal Deletion with a Novel Clan III-Restricted Avian Monoclonal Antibody: Exploiting Evolutionary Distance to Create Antibodies Specific for a Conserved VH Region Surface.
S. P. Cary, J. Lee, R. Wagenknecht, and G. J. Silverman (2000)
J. Immunol. 164, 4730-4741
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