کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1931772 | 1050563 | 2010 | 5 صفحه PDF | دانلود رایگان |

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-1QH1549.13 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 - Volume 394, Issue 4, 16 April 2010, Pages 904–908