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Slowly folding surface extension in the prototypic avian hepatitis B virus capsid governs stability.

<div class='caption-title'>Image reconstruction of CLPs vitrified 10 months after purification.</div>
<div class='caption-title'>Organization of HBc.</div>
<div class='caption-title'>Sample preparation and 2D-image analysis of DHBc 2 weeks and 10 months after purification.</div>
Makbul C, Nassal M, Böttcher B
OpenAccess logo Elife 9 (2020)
Cited: 13 times
EuropePMC logo PMID: 32795390

Abstract

Hepatitis B virus (HBV) is an important but difficult to study human pathogen. Most basics of the hepadnaviral life-cycle were unraveled using duck HBV (DHBV) as a model although DHBV has a capsid protein (CP) comprising ~260 rather than ~180 amino acids. Here we present high-resolution structures of several DHBV capsid-like particles (CLPs) determined by electron cryo-microscopy. As for HBV, DHBV CLPs consist of a dimeric α-helical frame-work with protruding spikes at the dimer interface. A fundamental new feature is a ~ 45 amino acid proline-rich extension in each monomer replacing the tip of the spikes in HBV CP. In vitro, folding of the extension takes months, implying a catalyzed process in vivo. DHBc variants lacking a folding-proficient extension produced regular CLPs in bacteria but failed to form stable nucleocapsids in hepatoma cells. We propose that the extension domain acts as a conformational switch with differential response options during viral infection.

Articles - 6ygh mentioned but not cited (4)

  1. Prediction of protein assemblies, the next frontier: The CASP14-CAPRI experiment. Lensink MF, Brysbaert G, Mauri T, Nadzirin N, Velankar S, Chaleil RAG, Clarence T, Bates PA, Kong R, Liu B, Yang G, Liu M, Shi H, Lu X, Chang S, Roy RS, Quadir F, Liu J, Cheng J, Antoniak A, Czaplewski C, Giełdoń A, Kogut M, Lipska AG, Liwo A, Lubecka EA, Maszota-Zieleniak M, Sieradzan AK, Ślusarz R, Wesołowski PA, Zięba K, Del Carpio Muñoz CA, Ichiishi E, Harmalkar A, Gray JJ, Bonvin AMJJ, Ambrosetti F, Vargas Honorato R, Jandova Z, Jiménez-García B, Koukos PI, Van Keulen S, Van Noort CW, Réau M, Roel-Touris J, Kotelnikov S, Padhorny D, Porter KA, Alekseenko A, Ignatov M, Desta I, Ashizawa R, Sun Z, Ghani U, Hashemi N, Vajda S, Kozakov D, Rosell M, Rodríguez-Lumbreras LA, Fernandez-Recio J, Karczynska A, Grudinin S, Yan Y, Li H, Lin P, Huang SY, Christoffer C, Terashi G, Verburgt J, Sarkar D, Aderinwale T, Wang X, Kihara D, Nakamura T, Hanazono Y, Gowthaman R, Guest JD, Yin R, Taherzadeh G, Pierce BG, Barradas-Bautista D, Cao Z, Cavallo L, Oliva R, Sun Y, Zhu S, Shen Y, Park T, Woo H, Yang J, Kwon S, Won J, Seok C, Kiyota Y, Kobayashi S, Harada Y, Takeda-Shitaka M, Kundrotas PJ, Singh A, Vakser IA, Dapkūnas J, Olechnovič K, Venclovas Č, Duan R, Qiu L, Xu X, Zhang S, Zou X, Wodak SJ. Proteins 89 1800-1823 (2021)
  2. Target highlights in CASP14: Analysis of models by structure providers. Alexander LT, Lepore R, Kryshtafovych A, Adamopoulos A, Alahuhta M, Arvin AM, Bomble YJ, Böttcher B, Breyton C, Chiarini V, Chinnam NB, Chiu W, Fidelis K, Grinter R, Gupta GD, Hartmann MD, Hayes CS, Heidebrecht T, Ilari A, Joachimiak A, Kim Y, Linares R, Lovering AL, Lunin VV, Lupas AN, Makbul C, Michalska K, Moult J, Mukherjee PK, Nutt WS, Oliver SL, Perrakis A, Stols L, Tainer JA, Topf M, Tsutakawa SE, Valdivia-Delgado M, Schwede T. Proteins 89 1647-1672 (2021)
  3. Slowly folding surface extension in the prototypic avian hepatitis B virus capsid governs stability. Makbul C, Nassal M, Böttcher B. Elife 9 e57277 (2020)
  4. Structural conservation of HBV-like capsid proteins over hundreds of millions of years despite the shift from non-enveloped to enveloped life-style. Pfister S, Rabl J, Wiegand T, Mattei S, Malär AA, Lecoq L, Seitz S, Bartenschlager R, Böckmann A, Nassal M, Boehringer D, Meier BH. Nat Commun 14 1574 (2023)


Reviews citing this publication (3)

  1. Solid-State NMR for Studying the Structure and Dynamics of Viral Assemblies. Lecoq L, Fogeron ML, Meier BH, Nassal M, Böckmann A. Viruses 12 E1069 (2020)
  2. The Hepatitis B Virus Nucleocapsid-Dynamic Compartment for Infectious Virus Production and New Antiviral Target. Niklasch M, Zimmermann P, Nassal M. Biomedicines 9 1577 (2021)
  3. HBV cccDNA-A Culprit and Stumbling Block for the Hepatitis B Virus Infection: Its Presence in Hepatocytes Perplexed the Possible Mission for a Functional Cure. Bhat SA, Kazim SN. ACS Omega 7 24066-24081 (2022)

Articles citing this publication (6)

  1. Assessment of the CASP14 assembly predictions. Ozden B, Kryshtafovych A, Karaca E. Proteins 89 1787-1799 (2021)
  2. Cryo-EM targets in CASP14. Cragnolini T, Kryshtafovych A, Topf M. Proteins 89 1949-1958 (2021)
  3. Conformational Plasticity of Hepatitis B Core Protein Spikes Promotes Peptide Binding Independent of the Secretion Phenotype. Makbul C, Khayenko V, Maric HM, Böttcher B. Microorganisms 9 956 (2021)
  4. Binding of a Pocket Factor to Hepatitis B Virus Capsids Changes the Rotamer Conformation of Phenylalanine 97. Makbul C, Kraft C, Grießmann M, Rasmussen T, Katzenberger K, Lappe M, Pfarr P, Stoffer C, Stöhr M, Wandinger AM, Böttcher B. Viruses 13 2115 (2021)
  5. Phosphorylation of the Hepatitis B Virus Large Envelope Protein. Fogeron ML, Lecoq L, Cole L, Montserret R, David G, Page A, Delolme F, Nassal M, Böckmann A. Front Mol Biosci 8 821755 (2021)
  6. Relaxing the restricted structural dynamics in the human hepatitis B virus RNA encapsidation signal enables replication initiation in vitro. Dörnbrack K, Beck J, Nassal M. PLoS Pathog 18 e1010362 (2022)


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