Redox control on the cell surface: implications for HIV-1 entry.
Proteins that work outside cells nearly always contain disulfide bonds. The prevailing view is that these bonds have been added during evolution to enhance protein stability. Recent evidence suggests that disulfide bonds can also control protein function. Certain secreted proteins contain one or more disulfide bonds that can control function by breaking and reforming in a controlled way. This review focuses on disulfide exchange events on the cell surface, with a particular reference to two proteins involved in HIV-1 infection. The primary HIV-1 receptor on immune cells, CD4, and the viral envelope glycoprotein, gp120, play a central role in HIV-1 entry. Redox change in a disulfide bond or bonds in one or both of these proteins appears to be important for HIV-1 entry.
Matthias
Lisa J
LJ
Centre for Vascular Research, University of New South Wales, Sydney, NSW 2052, Australia.
Hogg
Philip J
PJ
D019380:Anti-HIV Agents / Q000494:pharmacology; D015704:CD4 Antigens / Q000096:biosynthesis; D002462:Cell Membrane / Q000378:metabolism; D004220:Disulfides; D015699:HIV Envelope Protein gp120 / Q000378:metabolism; D015497:HIV-1 / Q000378:metabolism* / Q000502:physiology*; D006801:Humans; D010084:Oxidation-Reduction; D011485:Protein Binding; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013879:Thioredoxins / Q000378:metabolism
D019380:Anti-HIV Agents; D015704:CD4 Antigens; D004220:Disulfides; D015699:HIV Envelope Protein gp120; D013438:Sulfhydryl Compounds; D013879:Thioredoxins