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  • Clinician Researcher
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  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
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© Research
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature communications - 28 Jun 2022

Vaney MC, Dellarole M, Duquerroy S, Medits I, Tsouchnikas G, Rouvinski A, England P, Stiasny K, Heinz FX, Rey FA,

Link to Pubmed [PMID] – 35764616

Link to DOI – 10.1038/s41467-022-31111-y

Nat Commun 2022 Jun; 13(1): 3718

The flavivirus envelope glycoproteins prM and E drive the assembly of icosahedral, spiky immature particles that bud across the membrane of the endoplasmic reticulum. Maturation into infectious virions in the trans-Golgi network involves an acid-pH-driven rearrangement into smooth particles made of (prM/E)2 dimers exposing a furin site for prM cleavage into “pr” and “M”. Here we show that the prM “pr” moiety derives from an HSP40 cellular chaperonin. Furthermore, the X-ray structure of the tick-borne encephalitis virus (pr/E)2 dimer at acidic pH reveals the E 150-loop as a hinged-lid that opens at low pH to expose a positively-charged pr-binding pocket at the E dimer interface, inducing (prM/E)2 dimer formation to generate smooth particles in the Golgi. Furin cleavage is followed by lid-closure upon deprotonation in the neutral-pH extracellular environment, expelling pr while the 150-loop takes the relay in fusion loop protection, thus revealing the elusive flavivirus mechanism of fusion activation.

https://pubmed.ncbi.nlm.nih.gov/35764616