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CD4/immunoglobulin interaction: implications for immune physiology and autoimmunity.

P Lenert·M Zanetti
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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 V1 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 (p) 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.

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AnimalsAntigen-Antibody ComplexAutoimmunityCD4 AntigensHumansImmune SystemImmunoglobulin GJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.Review

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P Lenert, M Zanetti. 1991. CD4/immunoglobulin interaction: implications for immune physiology and autoimmunity.. https://doi.org/10.3109/08830189109061777

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