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Journal of Bioactive and Compatible Polymers, Vol. 19, No. 3, 173-195 (2004)
DOI: 10.1177/0883911504044456

Inhibition of U937 Cytokine Secretion by HIV-1 gp120 C4-Derived Peptide Constructs

Janet E. Kirkley

Program in Biochemistry, Knox College, Galesburg, IL 61401, USA jkirkley{at}knox.edu

Frank A. Robey

The Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA

Lipopolysaccharide (LPS) stimulation of the human promyelomonocytic cell line U937 results in interleukin 6 and interleukin 10 secretion. Modulation of cytokine secretion in response to LPS may be possible through binding of ligands to surface receptors. A peptomer, containing multiple repeat units of the CD4-binding C4 region of HIV-1 gp120, and the monomeric C4 peptide each were investigated for their ability to affect LPSinduced IL-6 and IL-10 secretion. The peptomer inhibited IL-6 and IL-10 secretion, while the monomer inhibited only IL-6 secretion. Larger CD4-binding proteins, specifically gp120 and Leu3A, a CD4-directed monoclonal antibody, had no effect on the LPS response. PMA differentiation to downregulate CD4 expression did not reverse the inhibitory effect of the peptomer or peptide, suggesting a CD4-independent effect. Bioactivity changed markedly with different constructs in the presence of IFN. with reversal or enhancement of the IL-10 response but not IL-6 production. These results suggest that truncation of a larger polypeptide may result in constructs with novel binding capabilities and bioactivities not seen in parent proteins.

Key Words: HIV • CD4 • peptomer • lipopolysaccharide • inflammation


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