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Cell. 1995 Jun 2;81(5):715-25.

Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex.

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Structural Biology Programme, European Molecular Biology Laboratory, Heidelberg Federal Republic of Germany.


Time-resolved cryoelectron microscopy reveals the first step in the conformational changes that enable membrane fusion in Semliki Forest virus. The neutral pH structure reveals a central cavity within the spike complex, plate-like extensions forming a layer above the membrane, and the paths of the paired transmembrane domains connecting the trimeric spikes and pentamer-hexamer clustered capsid subunits. Low pH treatment results in centrifugal movement of E2, the receptor-binding subunit, centripetal movement of E1 to narrow the central cavity initiating the formation of an E1 trimer, and the extension of the E1 fusion sequence toward the target membrane.

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