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2003 MAR 5 - (NewsRx.com & NewsRx.net) -- "The conserved surfaces of the human immunodeficiency virus (HIV)-1 envelope involved in receptor binding represent potential targets for the development of entry inhibitors and neutralizing antibodies. Using structural information on a CD4-gp120-17b antibody complex, we have designed a 27-amino acid CD4 mimic, CD4M33, that presents optimal interactions with gp120 and binds to viral particles and diverse HIV-1 envelopes with CD4-like affinity," researchers in France and Italy report.
"This mini-CD4 inhibits infection of both immortalized and primary cells by HIV-1, including primary patient isolates that are generally resistant to inhibition by soluble CD4," stated Loic Martin and colleagues at CEA Saclay, IRD/CNRS, and the Structural Biochemistry Center in France and at the San Raffaele Scientific Institute in Italy. "Furthermore, CD4M33 possesses functional properties of CD4, including the ability to unmask conserved neutralization epitopes of gp120 that are cryptic on the unbound glycoprotein."
The researchers ...