Structure and Function in Recombinant HIV-1 gp120 and Speculation about the Disulfide Bonding in the gp120 Homologs of HIV-2 and SIV
The envelope glyco-proteins of the primate immunodeficiency viruses (HIV-1, HIV-2 and SIV) have been the objects of intense study since their discovery. The major envelope glycoprotein (gp120 in HIV-1) is of particular interest because it mediates the attachment of the virus to susceptible cells via the CD4 molecule1,2, it contains most of the important epitopes for neutralization of the virus by antibodies3,4,5, it plays an important role in the process by which the viral and host cell membranes fuse and the viral capsid gains access to the cytoplasm6,7, and its sequence variability is central to the ability of the virus to adapt to and escape the protective immune response of the host organism8. Complete understanding of these processes requires an understanding of the molecular structure of gp120 in detail. Such structural information has proven to be difficult to obtain because of the large size of gp120 (approximately 480 amino acids), its high degree of glycosylation (approximately 50% by weight), the high degree of heterogeneity of the oligosaccharides on the molecule, and the scarcity of material available for analysis.
KeywordsCarbohydrate Mold Cysteine Carboxyl Disulfide
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