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Vol. 58, Issue 5, 982-992, November 2000
Laboratory of Drug Discovery Research and Development,
Developmental Therapeutics Program, Division of Cancer Treatment and
Diagnosis (B.R.O., S.P.S., J.M.M., M.J.C., M.R.B) and Structural
Biochemistry Program (D.X.), SAIC Frederick, Frederick Cancer Research
and Development Center, Frederick, Maryland; and Department of
Medicine, School of Medicine, University of Pennsylvania, Philadelphia,
Pennsylvania (W.Z., I.C.)
The novel virucidal protein cyanovirin-N (CV-N) binds with
equally high affinity to soluble forms of either H9 cell-produced or
recombinant glycosylated HIV-1 gp120 (sgp120) or gp160 (sgp160). Fluorescence polarization studies showed that CV-N is also capable of
binding to the glycosylated ectodomain of the HIV-envelope protein gp41
(sgp41) (as well as SIV glycoprotein 32), albeit with considerably
lower affinity than the sgp120/CV-N interaction. Pretreatment of CV-N
with either sgp120 or sgp41 abrogated the neutralizing activity of CV-N
against intact, infectious HIV-1 virions. Isothermal calorimetry and
optical biosensor binding studies showed that CV-N bound to recombinant
sgp120 with a Kd value ranging from 2 to 45 nM and to sgp41 with a Kd value of 606 nM;
furthermore, they indicated an approximate 5:1 stoichiometry for CV-N
binding to sgp120 and a 1:1 stoichiometry for CV-N binding to sgp41.
Circular dichroism studies additionally illuminated the binding of CV-N
with both sgp120 and sgp41, providing the first direct evidence that
conformational changes are a consequence of CV-N interactions with both
HIV-1 envelope glycoproteins.
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