A pocket-factor–triggered conformational switch in the hepatitis B virus capsid

Abstract: Viral hepatitis is growing into an epidemic illness, and it is urgent to neutralize the main culprit, hepatitis B virus (HBV), a small-enveloped retrotranscribing DNA virus. An intriguing observation in HB virion morphogenesis is that capsids with immature genomes are rarely enveloped and secreted. This prompted, in 1982, the postulate that a regulated conformation switch in the capsid triggers envelopment. Using solid-state NMR, we identified a stable alternative conformation of the capsid. The structural variations focus on the hydrophobic pocket of the core protein, a hot spot in capsid–envelope interactions. This structural switch is triggered by specific, high-affinity binding of a pocket factor. The conformational change induced by the binding is reminiscent of a maturation signal. This leads us to formulate the “synergistic double interaction” hypothesis, which explains the regulation of capsid envelopment and indicates a concept for therapeutic interference with HBV envelopment

Object Details

• Location: Deutsche Nationalbibliothek Frankfurt am Main
• Extent: Online-Ressource
• Language: Englisch
• Notes: Proceedings of the National Academy of Sciences of the United States of America. - 118, 17 (2021) , e2022464118, ISSN: 1091-6490

Contributors, Places and Time

• Event: Veröffentlichung
• (where): Freiburg
• (who): Universität
• (when): 2023
• Creator: Lecoq, Lauriane ; Wang, Shishan ; Dujardin, Marie ; Zimmermann, Peter ; Schuster, Leonard ; Fogeron, Marie-Laure ; Briday, Mathilde ; Schledorn, Maarten ; Wiegand, Thomas ; Cole, Laura ; Montserret, Roland ; Bressanelli, Stéphane ; Meier, Beat H. ; Nassal, Michael ; Böckmann, Anja

Further information

• DOI: 10.1073/pnas.2022464118
• URN: urn:nbn:de:bsz:25-freidok-2187854
• Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Last update: 25.03.2025, 1:43 PM CET