Evolution and activation mechanism of the flavivirus class ii membrane-fusion machinery

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SUMMARY

    The authors describe the X-ray structure of the soluble E (sE) dimer of TBEV in complex with pr at acidic pH, revealing a crucial role for the 150-loop of E domain I in relaying the fusion-loop capping role of pr upon secretion. Although the mass estimation for the sE fraction by MALS did not show an increase indicating that pr was bound to the sE dimer at acidic pH (Fig 1a, bottom panel), SDS-PAGE clearly showed that pr binds to the sE dimer at pH 5.5 but not at . . .

     

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