Journal article
Human CD4 binds immunoglobulins
Science (American Association for the Advancement of Science), Vol.248(4963), pp.1639-1643
06/29/1990
DOI: 10.1126/science.2363051
PMID: 2363051
Abstract
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.
Details
- Title: Subtitle
- Human CD4 binds immunoglobulins
- Creators
- Petar Lenert - Department of Medicine, University of California, San Diego 92103Daniel KroonHans SpiegelbergEdward S GolubMaurizio Zanetti
- Resource Type
- Journal article
- Publication Details
- Science (American Association for the Advancement of Science), Vol.248(4963), pp.1639-1643
- DOI
- 10.1126/science.2363051
- PMID
- 2363051
- NLM abbreviation
- Science
- ISSN
- 0036-8075
- eISSN
- 1095-9203
- Grant note
- AI 23871 / NIAID NIH HHS
- Language
- English
- Date published
- 06/29/1990
- Academic Unit
- Immunology; Internal Medicine
- Record Identifier
- 9984094643702771
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