Anti-equine tumor necrosis factor (tnf) activity of antisera raised against human tnf-α and peptide segments of human tnf

Robert J. MacKay From the Department of Large Animal Clinical Sciences, College of Veterinary Medicine, University of Florida, Gainesville, FL 32610 (MacKay), and Merck Sharp & Dohme Research Laboratories, West Point, PA 19486 (Socher).

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 BVSc, PhD
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Susan H. Socher From the Department of Large Animal Clinical Sciences, College of Veterinary Medicine, University of Florida, Gainesville, FL 32610 (MacKay), and Merck Sharp & Dohme Research Laboratories, West Point, PA 19486 (Socher).

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 PhD

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Summary

Antisera raised in rabbits against either purified recombinant-derived human tumor necrosis factor (tnf)- α (hutnf) or hutnf peptide-bovine thyroglobulin conjugates were evaluated for anti-equine tnf (eqtnf) activity. Binding and neutralizing anti-eqtnf activities were found in antisera raised against whole hutnf or against either of the peptides containing the N-terminal 15 amino acids of hutnf (hutnf[1-15] and hutnf[1-31]). Anti-eqtnf activity was not detected in antisera raised against hutnf[65-79], hutnf[98-111] or hutnf[124-141] peptides. The addition of excess hutnf[1-15] completely inhibited the ability of anti-hutnf[1-15] to bind eqtnf and reduced by approximately 25% the anti-eqtnf activity of an antiserum raised against whole hutnf. Nonconjugated hutnf[1-15] did not have eqtnf agonist or antagonist activity. Results were consistent with previous structural and functional data implicating the N-terminus of hutnf in receptor binding and indicate that the homologue of hutnf[1-15] on eqtnf may be a potentially important target for neutralizing anti-eqtnf antibodies.

Summary

Antisera raised in rabbits against either purified recombinant-derived human tumor necrosis factor (tnf)- α (hutnf) or hutnf peptide-bovine thyroglobulin conjugates were evaluated for anti-equine tnf (eqtnf) activity. Binding and neutralizing anti-eqtnf activities were found in antisera raised against whole hutnf or against either of the peptides containing the N-terminal 15 amino acids of hutnf (hutnf[1-15] and hutnf[1-31]). Anti-eqtnf activity was not detected in antisera raised against hutnf[65-79], hutnf[98-111] or hutnf[124-141] peptides. The addition of excess hutnf[1-15] completely inhibited the ability of anti-hutnf[1-15] to bind eqtnf and reduced by approximately 25% the anti-eqtnf activity of an antiserum raised against whole hutnf. Nonconjugated hutnf[1-15] did not have eqtnf agonist or antagonist activity. Results were consistent with previous structural and functional data implicating the N-terminus of hutnf in receptor binding and indicate that the homologue of hutnf[1-15] on eqtnf may be a potentially important target for neutralizing anti-eqtnf antibodies.

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