Bolmstedt, A., O'Keefe, B. R., Shenoy, S. R., McMahon, J. B., Boyd, M. R.: Mol.Pharmacol. 59: 949-954, 2001.
Abstract:
Here we demonstrate 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 (solely containing 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 while oligosaccharides smaller than Man-7 or monosaccharides did not interfere with CV-N/gp120 interaction, 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 thaty carry these oligosaccharides.
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