Macfarlane Burnet Institute for Medical Research and Public Health, Vic. 3004, Australia.
Biochem Biophys Res Commun. 2010 Apr 16;394(4):904-8. doi: 10.1016/j.bbrc.2010.03.071. Epub 2010 Mar 15.
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.
人类免疫缺陷病毒 1 型（HIV-1）融合糖蛋白 gp41 的保守二硫键结合区（DSR）介导与受体结合糖蛋白 gp120 的关联。gp120、CD4 和趋化因子受体之间的相互作用激活 gp41 的融合活性。将 HIV-1（QH1549.13）的 DSR 中的 W596L 和 W610F 突变引入，阻断了病毒进入和半融合，而不影响 gp120-gp41 结合。融合缺陷与 CD4 触发的 gp41 预发夹形成的抑制相关，这与 DSR 突变使 gp120 中的受体诱导构象变化与 gp41 激活脱钩一致。我们的数据表明 DSR 参与感测导致融合激活的 gp120-gp41 复合物中的构象变化。
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