[Structure and function of oligosaccharide chains of the envelope glycoprotein gp120 of human immunodeficiency virus type 1].
The surface of the human immunodeficiency virus (HIV-1), a causative agent for acquired immunodeficiency syndrome (AIDS), is covered with the major envelope glycoprotein gp120, of which the carbohydrate moiety accounted for 50% of the molecular mass. There is evidence that glycosylation of gp120 is prerequisite to the various stages of HIV infection. The oligosaccharide structures of gp120 have been determined using recombinant gp120 of HIV-1 (IIIB) produced in chinese hamster ovary cells and virus-derived gp120 isolated from H9 lymphocytes chronically infected with HIV-1 (IIIB). Three oligosaccharides have been suggested to be involved in the HIV-infection process. Occurrence of infection process which is independent of CD4 recognition and mediated by gp120 oligosaccharides, mannose-binding protein, and complement system has been suggested.
Mizuochi
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Institute for Comprehensive Medical Science, Fujita Health University School of Medicine.
D000163:Acquired Immunodeficiency Syndrome / Q000276:immunology / Q000378:metabolism; D000818:Animals; D002236:Carbohydrate Conformation; D006031:Glycosylation; D015699:HIV Envelope Protein gp120 / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D015497:HIV-1 / Q000378:metabolism* / Q000472:pathogenicity; D006801:Humans
D015699:HIV Envelope Protein gp120