scholarly journals Inhibition of human immunodeficiency virus (HIV) infection in vitro by anticarbohydrate monoclonal antibodies: peripheral glycosylation of HIV envelope glycoprotein gp120 may be a target for virus neutralization.

1990 ◽  
Vol 64 (6) ◽  
pp. 2833-2840 ◽  
Author(s):  
J E Hansen ◽  
H Clausen ◽  
C Nielsen ◽  
L S Teglbjaerg ◽  
L L Hansen ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Monoclonal Antibodies ◽  
Hiv Infection ◽  
Envelope Glycoprotein ◽  
Virus Neutralization ◽  
Envelope Glycoprotein Gp120 ◽  
Immunodeficiency Virus ◽  
Glycoprotein Gp120 ◽  
Hiv Envelope

scholarly journals Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development.

1997 ◽  
Vol 41 (7) ◽  
pp. 1521-1530 ◽  
Author(s):  
M R Boyd ◽  
K R Gustafson ◽  
J B McMahon ◽  
R H Shoemaker ◽  
B R O'Keefe ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Envelope Glycoprotein ◽  
Cell Types ◽  
Peripheral Blood Lymphocytes ◽  
Surface Envelope Glycoprotein ◽  
Envelope Glycoprotein Gp120 ◽  
Immunodeficiency Virus ◽  
Glycoprotein Gp120 ◽  
Surface Envelope ◽  
Viral Surface

We have isolated and sequenced a novel 11-kDa virucidal protein, named cyanovirin-N (CV-N), from cultures of the cyanobacterium (blue-green alga) Nostoc ellipsosporum. We also have produced CV-N recombinantly by expression of a corresponding DNA sequence in Escherichia coli. Low nanomolar concentrations of either natural or recombinant CV-N irreversibly inactivate diverse laboratory strains and primary isolates of human immunodeficiency virus (HIV) type 1 as well as strains of HIV type 2 and simian immunodeficiency virus. In addition, CV-N aborts cell-to-cell fusion and transmission of HIV-1 infection. Continuous, 2-day exposures of uninfected CEM-SS cells or peripheral blood lymphocytes to high concentrations (e.g., 9,000 nM) of CV-N were not lethal to these representative host cell types. The antiviral activity of CV-N is due, at least in part, to unique, high-affinity interactions of CV-N with the viral surface envelope glycoprotein gp120. The biological activity of CV-N is highly resistant to physicochemical denaturation, further enhancing its potential as an anti-HIV microbicide.

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