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. 1990 Jan;28(1):112–115. doi: 10.1128/jcm.28.1.112-115.1990

Synthetic peptide homologous to the envelope proteins of retroviruses shares a cross-reacting epitope with the CD4 receptor.

J Rothmann 1, N F Hassan 1, D E Campbell 1, N Kamani 1, S D Douglas 1
PMCID: PMC269547  PMID: 1688871

Abstract

A synthetic peptide (CKS-17) homologous to a highly conserved region of the retroviral transmembrane protein p15E was tested for its effect on receptor expression on monocytes. The CKS-17 amino acid sequence is present in several retroviruses including human T-cell lymphotropic virus types I and II and human immunodeficiency virus. The CKS-17 peptide has been previously shown to inhibit monocyte superoxide production, natural killer cell activity, polyclonal B-cell activation, and monocyte-mediated killing by inactivation of interleukin-1. In this study, we demonstrated that the anti-CD4 monoclonal antibody OKT4 binds strongly in vitro to CKS-17-treated human blood monocytes, whereas other antibodies tested were not reactive. This observed binding was the result of direct interaction of OKT4 antibody with the CKS-17 peptide. Moreover, a partial homology was found in amino acid sequence analysis of the CD4 epitope and the CKS-17 peptide.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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