Berkower I, Murphy D
Division of Allergenics and Parasitology Center for Biologics, FDA, NIH Campus, Bethesda, MD 20892.
Biochem Biophys Res Commun. 1993 Mar 31;191(3):1055-65. doi: 10.1006/bbrc.1993.1324.
We have found that the envelope glycoprotein gp120 of HIV-1 can be modified extensively by enzymatic oxidation of oligosaccharide chains without diminishing binding to its natural receptor, CD4. Using affinity purified galactose oxidase, over 20 sites per gp120 molecule were converted to chemically reactive aldehydes, as measured by 3H-BH4 reduction, while the conformation-dependent CD4 binding site remained intact. In contrast, periodate oxidation completely destroyed CD4 binding while producing fewer sites. Enzymatically labeled, biologically active gp120 should facilitate biochemical studies of receptor binding and viral inactivation by neutralizing antibodies.
