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. Author manuscript; available in PMC: 2018 Nov 4.
Published in final edited form as: Nat Struct Mol Biol. 2018 May 4;25(5):416–424. doi: 10.1038/s41594-018-0060-6

Figure 7.

Figure 7

The clamp-and-wedge model of HSV fusion. The CTD clamp restrains the gB ectodomain in its high-energy prefusion form. Binding of gD to one of its receptors (1) relieves it from an autoinhibited dimeric state (not shown) and results in activation of the gH/gL heterodimer (2). The ectodomain of activated gH/gL interacts with the gB ectodomain, while the gH cytotail releases the clamp by wedging between the intertwined CTD protomers (3). The destabilized clamp loses its hold on the ectodomain, and gB proceeds to refold into its thermodynamically favored postfusion conformation, drawing the virion and cell membranes together (4). The clamp then returns into its initial conformation (5).