Journal article
CD4/Immunoglobulin Interaction: Implications for Immune Physiology and Autoimmunity
International reviews of immunology, Vol.7(3), pp.237-244
1991
DOI: 10.3109/08830189109061777
PMID: 1757749
Abstract
CD4 has an important role in T cell activation events that depend on its binding to non-polymorphic MHC class II determinants on antigen-presenting cells. Here, we provide evidence that CD4 also interacts with immunoglobulins (Ig). The Ig-binding region lies within residues 21-49 of VI domain of CD4. Immunochemical studies suggest that this property of CD4 does not depend on the three-dimensional folding of the CD4 molecule. Synthetic peptides (/)) encompassing amino acid residues 16-49 and 21-49 of CD4 bind immunoglobulins in comparable way to the intact molecule. In vitro p 16-49 enhances significantly idiotype/anti-idiotype and some weak antigen-antibody interactions. Antigen antibody complexes formed in antigen excess bind CD4 peptides with much higher avidity then non-complexed antibodies. The possible role of the CD4/Ig interaction in T-B cell cooperation is discussed.
Details
- Title: Subtitle
- CD4/Immunoglobulin Interaction: Implications for Immune Physiology and Autoimmunity
- Creators
- Petar Lenert - University of California, San DiegoMaurizio Zanetti - University of California, San Diego
- Resource Type
- Journal article
- Publication Details
- International reviews of immunology, Vol.7(3), pp.237-244
- Publisher
- Informa UK Ltd
- DOI
- 10.3109/08830189109061777
- PMID
- 1757749
- ISSN
- 0883-0185
- eISSN
- 1563-5244
- Language
- English
- Date published
- 1991
- Academic Unit
- Immunology; Internal Medicine
- Record Identifier
- 9984359948802771
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