Abstract
Virology Rift Valley fever virus (RVFV) is transmitted by mosquitos and enters cells through receptor-mediated endocytosis. The infection process requires class II membrane fusion proteins, which insert a hydrophobic fusion loop into cell membranes and then refold. Guardado-Calvo et al. report the high-resolution crystal structure of RVFV class II fusion protein Gc in its postfusion form complexed with phosphatidylcholine. They find that Gc does not restructure its fusion loop after insertion. Rather, it uses an integrated system that accommodates glycerophospholipid head groups and then initiates membrane reorganization by concentrating cholesterol at the insertion site. Comparison with class II fusion proteins from other virus families suggests a common mechanism, which may provide a target for future antiviral therapies. Science , this issue p. [663][1] [1]: /lookup/doi/10.1126/science.aal2712
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