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The HIV-inactivating protein, cyanovirin-N, does not block gp120-mediated virus-to-cell binding
J M Mariner1, J B McMahon, B R O'Keefe
1Laboratory of Drug Discovery Research and Development, National Cancer Institute, Frederick Cancer Research & Development Center, Maryland 21702-1201, USA.
Biochemical and Biophysical Research Communications
|August 15, 1998
Summary
Cyanovirin-N (CV-N) effectively inactivates human immunodeficiency virus (HIV) by interfering with viral fusion after cell attachment. Unlike sCD4, CV-N inhibits infectivity without blocking initial binding or causing gp120 shedding.
Area of Science:
- Virology
- Immunology
- Biochemistry
Background:
- Cyanovirin-N (CV-N) is a potent protein with human immunodeficiency virus (HIV) inactivating properties.
- CV-N completely inhibits HIV-1 infectivity, but its mechanism of action requires further elucidation.
Purpose of the Study:
- To investigate the mechanism by which CV-N inhibits HIV-1 infectivity.
- To determine if CV-N interferes with the initial binding of HIV-1 to target cells or subsequent fusion steps.
Main Methods:
- Assessing the effect of CV-N on the binding of soluble CD4 (sCD4) to HIV-1 lysates.
- Evaluating the attachment of intact HIV-1 virions to target T-cell lines in the presence of CV-N.
- Analyzing viral ultrastructural changes and gp120 shedding upon CV-N treatment.
Main Results:
- CV-N did not block sCD4 binding to HIV-1 lysates.
- CV-N did not prevent intact HIV-1 virions from attaching to target T-cell lines.
- High concentrations of CV-N inactivated HIVRF without apparent shedding of gp120 or other ultrastructural changes, contrasting with sCD4 effects.
Conclusions:
- CV-N's virucidal effects stem from interfering with fusion steps subsequent to viral attachment to target cells.
- CV-N's mechanism differs from sCD4, as it does not disrupt viral envelope glycoproteins or initial binding.