Publications & Reports

Role for the disulfide-bonded region of human immunodeficiency virus type 1 gp41 in receptor-triggered activation of membrane fusion function.

Bellamy-McIntyre AK, Bär S, Ludlow L, Drummer HE, Poumbourios P
Macfarlane Burnet Institute for Medical Research and Public Health, Vic. 3004, Australia.


The conserved disulfide-bonded region (DSR) of the human immunodeficiency virus type 1 (HIV-1) fusion glycoprotein, gp41, mediates association with the receptor-binding glycoprotein, gp120. Interactions between gp120, CD4 and chemokine receptors activate the fusion activity of gp41. The introduction of W596L and W610F mutations to the DSR of HIV-1(QH1549.13) blocked viral entry and hemifusion without affecting gp120-gp41 association. The fusion defect correlated with inhibition of CD4-triggered gp41 pre-hairpin formation, consistent with the DSR mutations having decoupled receptor-induced conformational changes in gp120 from gp41 activation. Our data implicate the DSR in sensing conformational changes in the gp120-gp41 complex that lead to fusion activation.


  • Journal: Biochemical and Biophysical Research Communications
  • Published: 16/04/2010
  • Volume: 394
  • Issue: 4
  • Pagination: 904-908


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