|
|||||
|
|
Role for the disulfide-bonded region of human immunodeficiency virus type 1 gp41 in receptor-triggered activation of membrane fusion function |
|
| Authors: | Anna K Bellamy-McIntyre Séverine Bär Heidi E Drummer Pantelis Poumbourios |
| Institution: | a Macfarlane Burnet Institute for Medical Research and Public Health, Vic. 3004, Australia b Department of Microbiology, Monash University, Vic. 3168, Australia c Program Infection and Cancer, Abt. F010 and INSERM U701, Deutsches Krebsforschungszentrum, Heidelberg, Germany d Department of Microbiology and Immunology, The University of Melbourne, Vic. 3010, Australia |
| Abstract: | 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. |
| Keywords: | HIV-1 Receptor gp41 Disulfide-bonded region Membrane fusion |
| 本文献已被 ScienceDirect 等数据库收录！ | |