Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry.

Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry.

Blog Article

Membrane fusion is essential for entry of the biomedically-important paramyxoviruses into their host cells (viral-cell fusion), and for syncytia formation (cell-cell fusion), often induced by paramyxoviral infections [e.g.those of the deadly Nipah virus (NiV)].For most paramyxoviruses, membrane fusion requires two viral glycoproteins.

Upon receptor binding, the attachment glycoprotein (HN/H/G) triggers the fusion glycoprotein (F) to undergo conformational changes that merge viral and/or cell membranes.However, a significant knowledge gap remains on how HN/H/G couples cell receptor binding to F-triggering.Via interdisciplinary approaches we report the first comprehensive mechanism of NiV membrane fusion triggering, wella color charm 050 cooling violet involving three spatiotemporally sequential cell receptor-induced conformational steps in NiV-G: two in the head and one in the stalk.Interestingly, a headless NiV-G mutant was able to trigger NiV-F, and the two head conformational steps were required for the exposure of the stalk domain.

Moreover, the headless NiV-G prematurely triggered NiV-F on virions, indicating 2000 bmw 528i front bumper that the NiV-G head prevents premature triggering of NiV-F on virions by concealing a F-triggering stalk domain until the correct time and place: receptor-binding.Based on these and recent paramyxovirus findings, we present a comprehensive and fundamentally conserved mechanistic model of paramyxovirus membrane fusion triggering and cell entry.