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Atomic model of CPV reveals the mechanism used by this single-shelled virus to economically carry out functions conserved in multishelled reoviruses.

Yu X, Ge P, Jiang J, Atanasov I, Zhou ZH
Structure 19 652-61 (2011)
Cited: 46 times
EuropePMC logo PMID: 21565700

Abstract

Unlike the multishelled viruses in the Reoviridae, cytoplasmic polyhedrosis virus (CPV) is single shelled, yet stable and fully capable of carrying out functions conserved within Reoviridae. Here, we report a 3.1 Å resolution cryo electron microscopy structure of CPV and derive its atomic model, consisting of 60 turret proteins (TPs), 120 each of capsid shell proteins (CSPs) and large protrusion proteins (LPPs). Two unique segments of CSP contribute to CPV's stability: an inserted protrusion domain interacting with neighboring proteins, and an N-anchor tying up CSPs together through strong interactions such as β sheet augmentation. Without the need to interact with outer shell proteins, LPP retains only the N-terminal two-third region containing a conserved helix-barrel core and interacts exclusively with CSP. TP is also simplified, containing only domains involved in RNA capping. Our results illustrate how CPV proteins have evolved in a coordinative manner to economically carry out their conserved functions.

Articles - 3izx mentioned but not cited (9)

  1. Measurement of atom resolvability in cryo-EM maps with Q-scores. Pintilie G, Zhang K, Su Z, Li S, Schmid MF, Chiu W. Nat Methods 17 328-334 (2020)
  2. Atomic model of CPV reveals the mechanism used by this single-shelled virus to economically carry out functions conserved in multishelled reoviruses. Yu X, Ge P, Jiang J, Atanasov I, Zhou ZH. Structure 19 652-661 (2011)
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Reviews citing this publication (6)

  1. Single-Particle Cryo-EM at Crystallographic Resolution. Cheng Y. Cell 161 450-457 (2015)
  2. Limiting factors in atomic resolution cryo electron microscopy: no simple tricks. Zhang X, Zhou ZH. J Struct Biol 175 253-263 (2011)
  3. Problems in obtaining perfect images by single-particle electron cryomicroscopy of biological structures in amorphous ice. Henderson R, McMullan G. Microscopy (Oxf) 62 43-50 (2013)
  4. Electron Cryo-microscopy as a Tool for Structure-Based Drug Development. Merino F, Raunser S. Angew Chem Int Ed Engl 56 2846-2860 (2017)
  5. Electron Cryomicroscopy of Viruses at Near-Atomic Resolutions. Kaelber JT, Hryc CF, Chiu W. Annu Rev Virol 4 287-308 (2017)
  6. Mechanisms of Cell Entry by dsRNA Viruses: Insights for Efficient Delivery of dsRNA and Tools for Improved RNAi-Based Pest Control. Swevers L, Kontogiannatos D, Kolliopoulou A, Ren F, Feng M, Sun J. Front Physiol 12 749387 (2021)

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