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Structural Model of the Tubular Assembly of the Rous Sarcoma Virus Capsid Protein

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    Structural Model of the Tubular Assembly of the Rous Sarcoma Virus Capsid Protein
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    † Department of Physics, University of Central Florida, Orlando, Florida 32816, United States
    ‡ National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, United States
    § School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand
    ∥ Department of Microbiology and Immunology, Penn State University College of Medicine, Hershey, Pennsylvania 17033, United States
    ⊥ Department of Physics, Indiana University−Purdue University Indianapolis, Indianapolis, Indiana 46202, United States
    *[email protected]
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2017, 139, 5, 2006–2013
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    https://doi.org/10.1021/jacs.6b11939
    Published January 17, 2017
    Copyright © 2017 American Chemical Society
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    Abstract

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    The orthoretroviral capsid protein (CA) assembles into polymorphic capsids, whose architecture, assembly, and stability are still being investigated. The N-terminal and C-terminal domains of CA (NTD and CTD, respectively) engage in both homotypic and heterotypic interactions to create the capsid. Hexameric turrets formed by the NTD decorate the majority of the capsid surface. We report nearly complete solid-state NMR (ssNMR) resonance assignments of Rous sarcoma virus (RSV) CA, assembled into hexamer tubes that mimic the authentic capsid. The ssNMR assignments show that, upon assembly, large conformational changes occur in loops connecting helices, as well as the short 310 helix initiating the CTD. The interdomain linker becomes statically disordered. Combining constraints from ssNMR and cryo-electron microscopy (cryo-EM), we establish an atomic resolution model of the RSV CA tubular assembly using molecular dynamics flexible fitting (MDFF) simulations. On the basis of comparison of this MDFF model with an earlier-derived crystallographic model for the planar assembly, the induction of curvature into the RSV CA hexamer lattice arises predominantly from reconfiguration of the NTD–CTD and CTD trimer interfaces. The CTD dimer and CTD trimer interfaces are also intrinsically variable. Hence, deformation of the CA hexamer lattice results from the variable displacement of the CTDs that surround each hexameric turret. Pervasive H-bonding is found at all interdomain interfaces, which may contribute to their malleability. Finally, we find helices at the interfaces of HIV and RSV CA assemblies have very different contact angles, which may reflect differences in the capsid assembly pathway for these viruses.

    Copyright © 2017 American Chemical Society

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    Supporting Information

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/jacs.6b11939.

    • Summary of sample preparation; acquisition of ssNMR spectra; results of ssNMR assignments; cryo-EM conditions and MDFF simulations (PDF)

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    This article is cited by 7 publications.

    1. Chang Zhang, Wenjing Liu, Jing Deng, Shaojie Ma, Ziwei Chang, Jun Yang. Structural Insights into the Interaction between Bacillus subtilis SepF Assembly and FtsZ by Solid-State NMR Spectroscopy. The Journal of Physical Chemistry B 2022, 126 (28) , 5219-5230. https://doi.org/10.1021/acs.jpcb.2c02810
    2. Tyrone Thames, Alexander J. Bryer, Xin Qiao, Jaekyun Jeon, Ryan Weed, Kaylie Janicki, Bingwen Hu, Peter L. Gor’kov, Ivan Hung, Zhehong Gan, Juan R. Perilla, Bo Chen. Curvature of the Retroviral Capsid Assembly Is Modulated by a Molecular Switch. The Journal of Physical Chemistry Letters 2021, 12 (32) , 7768-7776. https://doi.org/10.1021/acs.jpclett.1c01769
    3. Chengyi Xu, Nabin Kandel, Xin Qiao, Md. Imran Khan, Preeta Pratakshya, Nadia E. Tolouei, Bo Chen, Alon A. Gorodetsky. Long-Range Proton Transport in Films from a Reflectin-Derived Polypeptide. ACS Applied Materials & Interfaces 2021, 13 (18) , 20938-20946. https://doi.org/10.1021/acsami.0c18929
    4. Bo Chen. ASAP: An automatic sequential assignment program for congested multidimensional solid state NMR spectra. Journal of Magnetic Resonance 2024, 361 , 107664. https://doi.org/10.1016/j.jmr.2024.107664
    5. Gal Porat-Dahlerbruch, Amir Goldbourt, Tatyana Polenova. Virus Structures and Dynamics by Magic-Angle Spinning NMR. Annual Review of Virology 2021, 8 (1) , 219-237. https://doi.org/10.1146/annurev-virology-011921-064653
    6. Basudev Maity, Zhipeng Li, Kento Niwase, Christian Ganser, Tadaomi Furuta, Takayuki Uchihashi, Diannan Lu, Takafumi Ueno. Single-molecule level dynamic observation of disassembly of the apo-ferritin cage in solution. Physical Chemistry Chemical Physics 2020, 22 (33) , 18562-18572. https://doi.org/10.1039/D0CP02069A
    7. Owen Pornillos, Barbie K Ganser-Pornillos. Maturation of retroviruses. Current Opinion in Virology 2019, 36 , 47-55. https://doi.org/10.1016/j.coviro.2019.05.004
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2017, 139, 5, 2006–2013
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jacs.6b11939
    Published January 17, 2017
    Copyright © 2017 American Chemical Society
    Request reuse permissions

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