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Vol. 59, Issue 5, 949-954, May 2001

ACCELERATED COMMUNICATION
Cyanovirin-N Defines a New Class of Antiviral Agent Targeting N-Linked, High-Mannose Glycans in an Oligosaccharide-Specific Manner

Anders J. Bolmstedt, Barry R. O'Keefe, Shilpa R. Shenoy, James B. McMahon, and Michael R. Boyd

Department of Clinical Virology, University of Göteborg, Sweden (A.J.B.) and Laboratory of Drug Discovery Research and Development, Division of Basic Sciences, National Cancer Institute, Frederick, Maryland (B.R.O., S.R.S., J.B.M., M.R.B.)

Herein we report that the novel HIV-inactivating protein cyanovirin-N (CV-N) targets specific, N-linked high-mannose oligosaccharides found on the viral envelope of HIV-1. First, we released the oligosaccharides by PnGase-treatment of HIV-gp120 (containing high-mannose, hybrid-type and complex-type oligosaccharides) or HSV-1 gC (containing only complex-type). Then, in an affinity chromatographic system, we found that CV-N bound to the free oligosaccharides from gp120 but not from gC-1, suggesting that high-mannose oligosaccharides constitute a target structure for CV-N. This was supported by the affinity of CV-N for high-mannose glycans released from gp120 by endo-H as well as high-mannose glycans released from castanospermine-treated HSV-1 gC. Furthermore, free Man-8 or Man-9 oligosaccharides partially inhibited the binding of CV-N to gp120, although neither oligosaccharides smaller than Man-7 nor monosaccharides interfered with CV-N/gp120 interaction, thereby establishing the oligosaccharide-specific affinity of CV-N to high-mannose glycans. This affinity for high-mannose oligosaccharides may explain the broad antiviral activity of CV-N against human and primate immunodeficiency retroviruses as well as certain other viruses that carry these oligosaccharides.

Copyright © 2001 by The American Society for Pharmacology and Experimental Therapeutics


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