The coronavirus spike protein is a multifunctional molecular machine that mediates coronavirus entry into host cells. It first binds to a receptor on the host cell surface through its S1 subunit and then fuses viral and host membranes through its S2 subunit. Two domains in S1 from different coronaviruses recognize a variety of host receptors, leading to viral attachment. The spike protein exists in two structurally distinct conformations, prefusion and postfusion. The transition from prefusion to postfusion conformation of the spike protein must be triggered, leading to membrane fusion. This article reviews current knowledge about the structures and functions of coronavirus spike proteins, illustrating how the two S1 domains recognize different receptors and how the spike proteins are regulated to undergo conformational transitions. I further discuss the evolution of these two critical functions of coronavirus spike proteins, receptor recognition and membrane fusion, in the context of the corresponding functions from other viruses and host cells.
|Original language||English (US)|
|Number of pages||25|
|Journal||Annual Review of Virology|
|State||Published - Sep 29 2016|
Bibliographical noteFunding Information:
ACKNOWLEDGMENTS: This work was supported by the National Institutes of Health (R01AI089728, R01AI110700).
© Copyright 2016 by Annual Reviews. All rights reserved.
Copyright 2017 Elsevier B.V., All rights reserved.
- Coronavirus spike protein
- Membrane fusion
- Postfusion conformation
- Prefusion conformation
- Receptor binding
- Virus evolution
- Virus origin