Functions of HIV envelope glycans.
The unusually highly glycosylated state of the major envelope glycoprotein (gp160) of the human immunodeficiency virus has offered a challenge to both glycobiologists and virologists. What is the functional significance of such a mass of glycans and how might they be manipulated to disadvantage virus pathogenesis? Some answers to each of these questions have already been obtained: N-linked glycans are necessary for the creation, but not the maintenance, of a bioactive conformation, and drug-induced alteration of the glycosylation pattern can lead to impaired virus infectivity. As a model for studying glycan function and as a target for antiviral therapy, gp160 represents a unique candidate.
Fenouillet
E
E
CNRS URA 1463, Paris, France.
Gluckman
J C
JC
Jones
I M
IM
D000818:Animals; D002240:Carbohydrate Sequence; D015686:Gene Products, env / Q000502:physiology*; D006023:Glycoproteins; D006031:Glycosylation; D006678:HIV / Q000502:physiology*; D015699:HIV Envelope Protein gp120 / Q000502:physiology; D019302:HIV Envelope Protein gp160; D015700:HIV Envelope Protein gp41 / Q000502:physiology; D006801:Humans; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000502:physiology*; D011498:Protein Precursors / Q000502:physiology*
D015686:Gene Products, env; D006023:Glycoproteins; D015699:HIV Envelope Protein gp120; D019302:HIV Envelope Protein gp160; D015700:HIV Envelope Protein gp41; D011134:Polysaccharides; D011498:Protein Precursors