Abstract
The members of the family Reoviridae (reoviruses) consist of 9–12 discrete double-stranded RNA (dsRNA) segments enclosed by single, double, or triple capsid layers. The outer capsid proteins of reoviruses exhibit the highest diversity in both sequence and structural organization. By contrast, the conserved RNA-dependent RNA polymerase (RdRp) structure in the conserved innermost shell in all reoviruses suggests that they share common transcriptional regulatory mechanisms. After reoviruses are delivered into the cytoplasm of a host cell, their inner capsid particles (ICPs) remain intact and serve as a stable nanoscale machine for RNA transcription and capping performed using enzymes in ICPs. Advances in cryo-electron microscopy have enabled the reconstruction at near-atomic resolution of not only the icosahedral capsid, including capping enzymes, but also the nonicosahedrally distributed complexes of RdRps within the capsid at different transcriptional stages. These near-atomic resolution structures allow us to visualize highly coordinated structural changes in the related enzymes, genomic RNA, and capsid protein during reovirus transcription. In addition, reoviruses encode their own enzymes for nascent RNA capping before RNA releasing from their ICPs.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Appleby TC, Perry JK, Murakami E, Barauskas O, Feng J, Cho A, Fox D 3rd, Wetmore DR, McGrath ME, Ray AS, Sofia MJ, Swaminathan S, Edwards TE (2015) Structural basis for RNA replication by the hepatitis C virus polymerase. Science 347(6223):771–775. https://doi.org/10.1126/science.1259210
Auguste AJ, Kaelber JT, Fokam EB, Guzman H, Carrington CV, Erasmus JH, Kamgang B, Popov VL, Jakana J, Liu X, Wood TG, Widen SG, Vasilakis N, Tesh RB, Chiu W, Weaver SC (2015) A newly isolated reovirus has the simplest genomic and structural organization of any reovirus. J Virol 89(1):676–687. https://doi.org/10.1128/JVI.02264-14
Bartlett NM, Gillies SC, Bullivan S, Bellamy AR (1974) Electron-microscopy study of reovirus reaction cores. J Virol 14(2):315–326
Borodavka A, Dykeman EC, Schrimpf W, Lamb DC (2017) Protein-mediated RNA folding governs sequence-specific interactions between rotavirus genome segments. eLife 6:e27453. https://doi.org/10.7554/eLife.27453
Borsa J, Graham AF (1968) Reovirus: RNA polymerase activity in purified virions. Biochem Biophys Res Commun 33(6):895–901. https://doi.org/10.1016/0006-291x(68)90396-3
Boyce M, Wehrfritz J, Noad R, Roy P (2004) Purified recombinant bluetongue virus VP1 exhibits RNA replicase activity. J Virol 78(8):3994–4002. https://doi.org/10.1128/jvi.78.8.3994-4002.2004
Bujnicki JM, Rychlewski L (2001) Reassignment of specificities of two cap methyltransferase domains in the reovirus lambda 2 protein. Genome Biol 2(9):RESEARCH0038
Carstens EB (2010) Ratification vote on taxonomic proposals to the international committee on taxonomy of viruses (2009). Arch Virol 155(1):133–146. https://doi.org/10.1007/s00705-009-0547-x
Chandran K, Walker SB, Chen Y, Contreras CM, Schiff LA, Baker TS, Nibert ML (1999) In vitro recoating of reovirus cores with baculovirus-expressed outer-capsid proteins mu1 and sigma3. J Virol 73(5):3941–3950. https://doi.org/10.1128/JVI.73.5.3941-3950.1999
Chang CT, Zweerink HJ (1971) Fate of parental reovirus in infected cell. Virology 46(3):544–555. https://doi.org/10.1016/0042-6822(71)90058-4
Chen JZ, Settembre EC, Aoki ST, Zhang X, Bellamy AR, Dormitzer PR, Harrison SC, Grigorieff N (2009) Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM. Proc Natl Acad Sci U S A 106(26):10644–10648. https://doi.org/10.1073/pnas.0904024106
Cheng L (2015) Cryo-EM shows the polymerase structures and a non-spooled genome within a dsRNA virus. In: International Mini-Symposium of Structural Virology, Beijing, China, April 9th 2015
Cheng L, Fang Q, Shah S, Atanasov IC, Zhou ZH (2008) Subnanometer-resolution structures of the grass carp reovirus core and virion. J Mol Biol 382(1):213–222
Cheng L, Zhu J, Hui WH, Zhang XK, Honig B, Fang Q, Zhou ZH (2010) Backbone model of an aquareovirus virion by cryo-electron microscopy and bioinformatics. J Mol Biol 397(3):852–863. https://doi.org/10.1016/j.jmb.2009.12.027
Cheng L, Sun J, Zhang K, Mou Z, Huang X, Ji G, Sun F, Zhang J, Zhu P (2011) Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping. Proc Natl Acad Sci U S A 108(4):1373–1378. https://doi.org/10.1073/pnas.1014995108
Coulibaly F, Chiu E, Ikeda K, Gutmann S, Haebel PW, Schulze-Briese C, Mori H, Metcalf P (2007) The molecular organization of cypovirus polyhedra. Nature 446(7131):97–101. https://doi.org/10.1038/Nature05628
Crawford SE, Mukherjee SK, Estes MK, Lawton JA, Shaw AL, Ramig RF, Prasad BV (2001) Trypsin cleavage stabilizes the rotavirus VP4 spike. J Virol 75(13):6052–6061. https://doi.org/10.1128/JVI.75.13.6052-6061.2001
Cui Y, Zhang Y, Zhou K, Sun J, Zhou ZH (2019) Conservative transcription in three steps visualized in a double-stranded RNA virus. Nat Struct Mol Biol 26(11):1023–1034. https://doi.org/10.1038/s41594-019-0320-0
Dai X, Li Z, Lai M, Shu S, Du Y, Zhou ZH, Sun R (2017) In situ structures of the genome and genome-delivery apparatus in a single-stranded RNA virus. Nature 541(7635):112–116. https://doi.org/10.1038/nature20589
de Gennes PG, Prost J (1993) The physics of liquid crystals. Oxford University Press, Oxford
Decroly E, Ferron F, Lescar J, Canard B (2012) Conventional and unconventional mechanisms for capping viral mRNA. Nat Rev Microbiol 10(1):51–65. https://doi.org/10.1038/nrmicro2675.nrmicro2675[pii]
Ding K, Nguyen L, Zhou ZH (2018) In situ structures of the polymerase complex and RNA genome show how Aquareovirus transcription machineries respond to Uncoating. J Virol 92(21):e00774-18. https://doi.org/10.1128/JVI.00774-18
Ding K, Celma CC, Zhang X, Chang T, Shen W, Atanasov I, Roy P, Zhou ZH (2019) In situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release. Nat Commun 10(1):2216. https://doi.org/10.1038/s41467-019-10236-7
Drayna D, Fields BN (1982) Activation and characterization of the reovirus transcriptase: genetic analysis. J Virol 41(1):110–118. https://doi.org/10.1128/JVI.41.1.110-118.1982
Dryden KA, Wang GJ, Yeager M, Nibert ML, Coombs KM, Furlong DB, Fields BN, Baker TS (1993) Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation - analysis of virions and dubviral particles by cryoelectron microscopy and image-reconstruction. J Cell Biol 122(5):1023–1041
Farsetta DL, Chandran K, Nibert ML (2000) Transcriptional activities of reovirus RNA polymerase in recoated cores. Initiation and elongation are regulated by separate mechanisms. J Biol Chem 275(50):39693–39701. https://doi.org/10.1074/jbc.M004562200
Fausnaugh J, Shatkin AJ (1990) Active site localization in a viral mRNA capping enzyme. J Biol Chem 265(13):7669–7672
Ferrer-Orta C, Arias A, Escarmis C, Verdaguer N (2006) A comparison of viral RNA-dependent RNA polymerases. Curr Opin Struct Biol 16(1):27–34. https://doi.org/10.1016/j.sbi.2005.12.002
Furuichi Y (1974) “Methylation-coupled” transcription by virus-associated transcriptase of cytoplasmic polyhedrosis virus containing double-stranded RNA. Nucleic Acids Res 1(6):809–822. https://doi.org/10.1093/nar/1.6.809
Furuichi Y (1978) “Pretranscriptional capping” in the biosynthesis of cytoplasmic polyhedrosis virus mRNA. Proc Natl Acad Sci U S A 75(3):1086–1090. https://doi.org/10.1073/pnas.75.3.1086
Furuichi Y, Miura K (1975) A blocked structure at the 5′ terminus of mRNA from cytoplasmic polyhedrosis virus. Nature 253(5490):374–375
Gillies S, Bullivant S, Bellamy AR (1971) Viral RNA polymerases: electron microscopy of reovirus reaction cores. Science 174(4010):694–696. https://doi.org/10.1126/science.174.4010.694
Gouet P, Diprose JM, Grimes JM, Malby R, Burroughs JN, Zientara S, Stuart DI, Mertens PPC (1999) The highly ordered double-stranded RNA genome of bluetongue virus revealed by crystallography. Cell 97(4):481–490
Grimes JM, Burroughs JN, Gouet P, Diprose JM, Malby R, Zientara S, Mertens PPC, Stuart DI (1998) The atomic structure of the bluetongue virus core. Nature 395(6701):470–478
Harrus D, Ahmed-El-Sayed N, Simister PC, Miller S, Triconnet M, Hagedorn CH, Mahias K, Rey FA, Astier-Gin T, Bressanelli S (2010) Further insights into the roles of GTP and the C terminus of the hepatitis C virus polymerase in the initiation of RNA synthesis. J Biol Chem 285(43):32906–32918. https://doi.org/10.1074/jbc.M110.151316
He Y, Shivakoti S, Ding K, Cui Y, Roy P, Zhou ZH (2019) In situ structures of RNA-dependent RNA polymerase inside bluetongue virus before and after uncoating. Proc Natl Acad Sci U S A 116(33):16535–16540. https://doi.org/10.1073/pnas.1905849116
Ilca SL, Sun X, El Omari K, Kotecha A, de Haas F, DiMaio F, Grimes JM, Stuart DI, Poranen MM, Huiskonen JT (2019) Multiple liquid crystalline geometries of highly compacted nucleic acid in a dsRNA virus. Nature 570(7760):252–256. https://doi.org/10.1038/s41586-019-1229-9
Jenni S, Salgado EN, Herrmann T, Li Z, Grant T, Grigorieff N, Trapani S, Estrozi LF, Harrison SC (2019) In situ structure of rotavirus VP1 RNA-dependent RNA polymerase. J Mol Biol 431(17):3124–3138. https://doi.org/10.1016/j.jmb.2019.06.016
Kaelber JT, Jiang W, Weaver SC, Auguste AJ, Chiu W (2020) Arrangement of the polymerase complexes inside a nine-segmented dsRNA virus. Structure 28 (6):604-612, e603. https://doi.org/10.1016/j.str.2020.01.011
Kim J, Parker JS, Murray KE, Nibert ML (2004) Nucleoside and RNA triphosphatase activities of orthoreovirus transcriptase cofactor mu2. J Biol Chem 279(6):4394–4403. https://doi.org/10.1074/jbc.M308637200
King AMQ, Adams MJ, Carstens EB, Lefkowitz EJ (2011) Virus taxonomy. Ninth report of the international committee on taxonomy of viruses. Elsevier Inc., London
Kumar D, Yu X, Crawford SE, Moreno R, Jakana J, Sankaran B, Anish R, Kaundal S, Hu L, Estes MK, Wang Z, Prasad BVV (2020) 2.7 a cryo-EM structure of rotavirus core protein VP3, a unique capping machine with a helicase activity. Sci Adv 6(16):eaay6410. https://doi.org/10.1126/sciadv.aay6410
Lawton JA, Estes MK, Prasad BVV (1997) Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles. Nat Struct Biol 4(2):118–121
Lee PW, Hayes EC, Joklik WK (1981) Protein sigma 1 is the reovirus cell attachment protein. Virology 108(1):156–163. https://doi.org/10.1016/0042-6822(81)90535-3
Levin DH, Mendelsohn N, Schonberg M, Klett H, Silverstein S, Kapuler AM, Acs G (1970) Properties of RNA transcriptase in reovirus subviral particles. Proc Natl Acad Sci U S A 66(3):890–897. https://doi.org/10.1073/pnas.66.3.890
Li X, Zhou N, Chen W, Zhu B, Wang X, Xu B, Wang J, Liu H, Cheng L (2017) Near-atomic resolution structure determination of a cypovirus capsid and polymerase complex using cryo-EM at 200kV. J Mol Biol 429(1):79–87
Li X, Wang L, Wang X, Chen W, Yang T, Song J, Liu H, Cheng L (2020) Structure of RdRps within a transcribing dsRNA virus provides insights into the mechanisms of RNA synthesis. J Mol Biol 432(2):358–366. https://doi.org/10.1016/j.jmb.2019.09.015
Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC (2002) Structure of the reovirus membrane-penetration protein, mu 1, in a complex with its protector protein, sigma 3. Cell 108(2):283–295
Liu H (2015) Symmetry-mismatch reconstruction for icosahedral viruses. In: International Mini-Symposium of Structural Virology, Beijing, China, April 9th 2015
Liu H, Cheng L (2015) Cryo-EM shows the polymerase structures and a nonspooled genome within a dsRNA virus. Science 349(6254):1347–1350. https://doi.org/10.1126/science.aaa4938
Lu X, McDonald SM, Tortorici MA, Tao YJ, Vasquez-Del Carpio R, Nibert ML, Patton JT, Harrison SC (2008) Mechanism for coordinated RNA packaging and genome replication by rotavirus polymerase VP1. Structure 16(11):1678–1688. https://doi.org/10.1016/j.str.2008.09.006
Luongo CL, Contreras CM, Farsetta DL, Nibert ML (1998) Binding site for S-adenosyl-L-methionine in a central region of mammalian reovirus lambda 2 protein - evidence for activities in mRNA CAP methylation. J Biol Chem 273(37):23773–23780
Luongo CL, Reinisch KM, Harrison SC, Nibert ML (2000) Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda 2. J Biol Chem 275(4):2804–2810
McClain B, Settembre E, Temple BRS, Bellamy AR, Harrison SC (2010) X-ray crystal structure of the rotavirus inner capsid particle at 3.8 angstrom resolution. J Mol Biol 397(2):587–599. https://doi.org/10.1016/j.jmb.2010.01.055
McDonald SM, Tao YJ, Patton JT (2009) The ins and outs of four-tunneled Reoviridae RNA-dependent RNA polymerases. Curr Opin Struct Biol 19(6):775–782. https://doi.org/10.1016/j.sbi.2009.10.007
Mendez II, Weiner SG, She YM, Yeager M, Coombs KM (2008) Conformational changes accompany activation of reovirus RNA-dependent RNA transcription. J Struct Biol 162(2):277–289. https://doi.org/10.1016/j.jsb.2008.01.006
Mertens P (2004) The dsRNA viruses. Virus Res 101(1):3–13
Miyazaki N, Uehara-Ichiki T, Xing L, Bergman L, Higashiura A, Nakagawa A, Omura T, Cheng RH (2008) Structural evolution of reoviridae revealed by oryzavirus in acquiring the second capsid shell. J Virol 82(22):11344–11353
Nibert ML, Baker TS (2003) CPV, a stable and symmetrical machine for mRNA synthesis. Structure 11(6):605–607. https://doi.org/10.1016/S0969-2126(03)00099-6
Nibert ML, Fields BN (1992) A carboxy-terminal fragment of protein mu 1/mu 1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration. J Virol 66(11):6408–6418. https://doi.org/10.1128/JVI.66.11.6408-6418.1992
Nibert ML, Kim J (2004) Conserved sequence motifs for nucleoside triphosphate binding unique to turreted reoviridae members and coltiviruses. J Virol 78(10):5528–5530
Nibert ML, Furlong DB, Fields BN (1991a) Mechanisms of viral pathogenesis. Distinct forms of reoviruses and their roles during replication in cells and host. J Clin Invest 88(3):727–734. https://doi.org/10.1172/JCI115369
Nibert ML, Schiff LA, Fields BN (1991b) Mammalian reoviruses contain a myristoylated structural protein. J Virol 65(4):1960–1967. https://doi.org/10.1128/JVI.65.4.1960-1967.1991
Noble S, Nibert ML (1997) Core protein mu2 is a second determinant of nucleoside triphosphatase activities by reovirus cores. J Virol 71(10):7728–7735
Odegard AL, Chandran K, Zhang X, Parker JS, Baker TS, Nibert ML (2004) Putative autocleavage of outer capsid protein micro1, allowing release of myristoylated peptide micro1N during particle uncoating, is critical for cell entry by reovirus. J Virol 78(16):8732–8745. https://doi.org/10.1128/JVI.78.16.8732-8745.2004
Patton JT, Jones MT, Kalbach AN, He YW, Xiaobo J (1997) Rotavirus RNA polymerase requires the core shell protein to synthesize the double-stranded RNA genome. J Virol 71(12):9618–9626
Periz J, Celma C, Jing B, Pinkney JN, Roy P, Kapanidis AN (2013) Rotavirus mRNAS are released by transcript-specific channels in the double-layered viral capsid. Proc Natl Acad Sci U S A 110(29):12042–12047. https://doi.org/10.1073/pnas.1220345110
Pesavento JB, Lawton JA, Estes MK, Prasad BVV (2001) The reversible condensation and expansion of the rotavirus genome. P Natl Acad Sci USA 98(4):1381–1386
Reinisch KM, Nibert M, Harrison SC (2000) Structure of the reovirus core at 3.6 angstrom resolution. Nature 404(6781):960–967
Roy P (2017) Bluetongue virus structure and assembly. Curr Opin Virol 24:115–123. https://doi.org/10.1016/j.coviro.2017.05.003
Scrima N, Caillet-Saguy C, Ventura M, Harrus D, Astier-Gin T, Bressanelli S (2012) Two crucial early steps in RNA synthesis by the hepatitis C virus polymerase involve a dual role of residue 405. J Virol 86(13):7107–7117. https://doi.org/10.1128/JVI.00459-12
Settembre EC, Chen JZ, Dormitzer PR, Grigorieff N, Harrison SC (2011) Atomic model of an infectious rotavirus particle. EMBO J 30(2):408–416. https://doi.org/10.1038/emboj.2010.322
Shatkin AJ, Sipe JD (1968) RNA polymerase activity in purified reoviruses. Proc Natl Acad Sci U S A 61(4):1462–1469. https://doi.org/10.1073/pnas.61.4.1462
Silverstein SC, Schonberg M, Levin DH, Acs G (1970) The reovirus replicative cycle: conservation of parental RNA and protein. Proc Natl Acad Sci U S A 67(1):275–281. https://doi.org/10.1073/pnas.67.1.275
Skehel JJ, Joklik WK (1969) Studies on the in vitro transcription of reovirus RNA catalyzed by reovirus cores. Virology 39(4):822–831. https://doi.org/10.1016/0042-6822(69)90019-1
Smith RE, Furuichi Y (1980) Gene mapping of cytoplasmic polyhedrosis virus of silkworm by the full-length mRNA prepared under optimized conditions of transcription in vitro. Virology 103(2):279–290
Starnes MC, Joklik WK (1993) Reovirus protein lambda 3 is a poly(C)-dependent poly(G) polymerase. Virology 193(1):356–366. https://doi.org/10.1006/viro.1993.1132
Sutton G, Grimes JM, Stuart DI, Roy P (2007) Bluetongue virus VP4 is an RNA-capping assembly line. Nat Struct Mol Biol 14(5):449–451. https://doi.org/10.1038/nsmb1225
Tao YZ, Farsetta DL, Nibert ML, Harrison SC (2002) RNA synthesis in a cage - structural studies of reovirus polymerase lambda 3. Cell 111(5):733–745
Trask SD, McDonald SM, Patton JT (2012) Structural insights into the coupling of virion assembly and rotavirus replication. Nat Rev Microbiol 10(3):165–177. https://doi.org/10.1038/nrmicro2673
Van Dijk AA, Huismans H (1980) The in vitro activation and further characterization of the bluetongue virus-associated transcriptase. Virology 104(2):347–356. https://doi.org/10.1016/0042-6822(80)90339-6
Wang X, Zhang F, Su R, Li X, Chen W, Chen Q, Yang T, Wang J, Liu H, Fang Q, Cheng L (2018) Structure of RNA polymerase complex and genome within a dsRNA virus provides insights into the mechanisms of transcription and assembly. Proc Natl Acad Sci U S A 115(28):7344–7349. https://doi.org/10.1073/pnas.1803885115
Wehrfritz JM, Boyce M, Mirza S, Roy P (2007) Reconstitution of bluetongue virus polymerase activity from isolated domains based on a three-dimensional structural model. Biopolymers 86(1):83–94. https://doi.org/10.1002/bip.20706
Yan XD, Parent KN, Goodman RP, Tang JH, Shou JY, Nibert ML, Duncan R, Baker TS (2011) Virion structure of baboon reovirus, a fusogenic orthoreovirus that lacks an adhesion fiber. J Virol 85(15):7483–7495. https://doi.org/10.1128/Jvi.00729-11
Yang C, Ji G, Liu H, Zhang K, Liu G, Sun F, Zhu P, Cheng L (2012) Cryo-EM structure of a transcribing cypovirus. Proc Natl Acad Sci U S A 109(16):6118–6123. https://doi.org/10.1073/pnas.1200206109
Yu X, Jiang J, Sun J, Zhou ZH (2015) A putative ATPase mediates RNA transcription and capping in a dsRNA virus. eLife 4:e07901. https://doi.org/10.7554/eLife.07901
Zeng CQ, Estes MK, Charpilienne A, Cohen J (1998) The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3. J Virol 72(1):201–208. https://doi.org/10.1128/JVI.72.1.201-208.1998
Zhang X, Walker SB, Chipman PR, Nibert ML, Baker TS (2003) Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 angstrom. Nat Struct Biol 10(12):1011–1018. https://doi.org/10.1038/Nsb1009
Zhang X, Ji Y, Zhang L, Harrison SC, Marinescu DC, Nibert ML, Baker TS (2005a) Features of reovirus outer capsid protein mu1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 angstrom resolution. Structure 13(10):1545–1557. https://doi.org/10.1016/j.str.2005.07.012
Zhang X, Tang JH, Walker SB, O’Hara D, Nibert ML, Duncan R, Baker TS (2005b) Structure of avian orthoreovirus virion by electron cryomicroscopy and image reconstruction. Virology 343(1):25–35. https://doi.org/10.1016/j.virol.2005.08.002
Zhang X, Jin L, Fang Q, Hui WH, Zhou ZH (2010) 3.3 angstrom Cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 141(3):472–482
Zhang X, Ding K, Yu X, Chang W, Sun J, Zhou ZH (2015) In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus. Nature 527(7579):531–534. https://doi.org/10.1038/nature15767
Zhang X, Patel A, Celma CC, Yu X, Roy P, Zhou ZH (2016) Atomic model of a nonenveloped virus reveals pH sensors for a coordinated process of cell entry. Nat Struct Mol Biol 23(1):74–80. https://doi.org/10.1038/nsmb.3134
Zhou ZH, Zhang H, Jakana J, Lu XY, Zhang JQ (2003) Cytoplasmic polyhedrosis virus structure at 8 angstrom by electron cryomicroscopy: structural basis of capsid stability and mRNA processing regulation. Structure 11(6):651–663. https://doi.org/10.1016/S0969-2126(03)00091-1
Zhu B, Yang C, Liu H, Cheng L, Song F, Zeng S, Huang X, Ji G, Zhu P (2014) Identification of the active sites in the methyltransferases of a transcribing dsRNA virus. J Mol Biol 426(11):2167–2174. https://doi.org/10.1016/j.jmb.2014.03.013
Acknowledgements
This research was supported by the National Natural Science Foundation of China (12034006, 31971122, and 32071209).
Author information
Authors and Affiliations
Corresponding authors
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2022 The Author(s), under exclusive license to Springer Nature Switzerland AG
About this chapter
Cite this chapter
Liu, H., Cheng, L. (2022). Viral Capsid and Polymerase in Reoviridae. In: Harris, J.R., Marles-Wright, J. (eds) Macromolecular Protein Complexes IV. Subcellular Biochemistry, vol 99. Springer, Cham. https://doi.org/10.1007/978-3-031-00793-4_17
Download citation
DOI: https://doi.org/10.1007/978-3-031-00793-4_17
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-031-00792-7
Online ISBN: 978-3-031-00793-4
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)