1. Synthetic peptide homologous to the envelope proteins of retroviruses shares a cross-reacting epitope with the CD4 receptor
- Author
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N F Hassan, J Rothmann, Naynesh Kamani, Steven D. Douglas, and Donald E. Campbell
- Subjects
Microbiology (medical) ,medicine.drug_class ,Receptor expression ,Molecular Sequence Data ,Retroviridae Proteins ,Peptide ,Cross Reactions ,In Vitro Techniques ,Monoclonal antibody ,Epitope ,Monocytes ,Epitopes ,Viral envelope ,Viral Envelope Proteins ,medicine ,Humans ,Amino Acid Sequence ,Peptide sequence ,Antigens, Viral ,Cell Line, Transformed ,chemistry.chemical_classification ,biology ,Antibodies, Monoclonal ,Molecular biology ,chemistry ,Polyclonal antibodies ,CD4 Antigens ,biology.protein ,Antibody ,Peptides ,Research Article - 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.
- Published
- 1990