The Positive Sense Single Stranded RNA Viruses

Duin, Jan van; Wor, S. van den; Buck, K. W.; Esteban, Rosa; Hillman, Bradley I.; Stanway, Glyn; Brown, F.; Christian, Peter D.; Hovi, Tapani; Hyypiä, Timo; King, Andrew M. Q.; Knowles, N. J.; Lemon, Stanley M.; Minor, P. D.; Pallansch,; Palmenberg, A C; Skern, Tim; Carstens, Eric B.; Johnson, Karyn N.; Nakashima, Nobuhiko; Scotti, Paul D.; Wilk, F. van der; Culley, Alexander I.; Lang, Andrew S.; Suttle, Curtis A.; Gall, Olivier Le; Iwanami, Toru; Jones, Taylor; Lehto, Kirsi; Sanfaçon, Hélène; Wellink, J.; Wetzel, Thierry; Yoshikawa, Nobuyuki; Berger, P. H.; Adams, M. J.; Barnett, O. W.; Brunt, A.A.; Hammond, John A.; Hill, John H.; Jordan, R.; Kashiwazaki, Satoshi; Rybicki, Edward P.; Spence, Nicola; Stenger, Drake C.; Ohki, Satoshi T.; Uyeda, Ichiro; Zaayen, A. van; Valkonen, Jari P. T.; Vetten, H. J.; Koopmans, Marion; Green, K.Y.; Ando, Tamie; Clarke, Ian N.; Estes, M K; Matson, David O.; Nakata, Shuji; Neill, John D.; Smith, Alvin W.; Studdert, Michael J.; Thiel, Heike; Emerson, Suzanne U.; Anderson, Dallas W.; A, Arankalle; Meng, Xiang‐Jin; Purdy, Michael A.; Schlauder, George G.; Tsarev, Sergei A.; Monroe, Stephan S.; Carter, M.J; Herrmann, John E.; Mitchel, D.K.; Sánchez-Fauquier, Alicia; Schneemann, Anette; Delsert, Claude; Johnson, John E.; Nishizawa, Tsutomu; Hanzlik, Terry N.; Gordon, Karl; Gorbalenya, Alexander E.; Hendry, D. A.; Pringle, Fiona M.; Ward, Vernon K.; Zeddam, Jean Louis; Hull, Roger; Fargette, Denis; D’Arcy, Cleora J.; Domier, Leslie L.; Taliansky, Michael; Robinson, D. J.; Waterhouse, Peter M.; Murant, A. F.; Zoeten, G. A. de; Falk, Bryce W.; Gibbs, Mark J.; Lommel, Steven A.; Martelli, G. P.; Rubino, Luisa; Russo, Marcello; Spaan, Willy J. M.; Cavanagh, David; Groot, Raoul J. de; Enjuanes, Luis; Snijder, Eric J.; Walker, Peter; Brian, David A.; Holmes, Kathryn V.; Masters, Paul S.; Rottier, Peter J. M.; Taguchi, Fumihiro; Talbot, Pierre J.; Brinton,; Faaberg, Kay S.; Godeny, Elmer K.; Maclachlan, Nigel J; Mengeling, W. L.; Plagemann, Peter G.W.; Bonami, Jean Robert; Boonsaeng,; Chang, Poh-Shing; Cowley, Jeff A.; Flegel, Timothy W.; Lightner, Donald V.; Loh, Philip C.; Tang, Kathy F.J.; Collett,; Gould, E. A.; Heinz, Franz X.; Houghton, Michael; Meyers, Gregor; Purcell, Robert H.; Rice, Claire M; Weaver, Scott C.; Frey, Teryl K.; Huang, Hsing‐I; Kinney, Richard M.; Roehrig, John T.; Shope, Robert E.; Strauss, Ellen G.; Lewandowski, Dennis J.; Bragg, Jennifer; Solovyev, A.G.; Morozov, Sergey Y.; Atabekov, J.G.; Jackson, A.O.; Torrance, L.; Koenig, R.; Lesemann, D.‐E.; Richards, K.; Deom, C. M.; Naidu, Rayapati A.; Roossinck, Marilyn J.; Bujarski, Józef J.; Ding, Shou‐Wei; Hajimorad, R.; Hanada, Kaoru; Scott, Seth D.; Tousignant, M. E.; Milne, Robert G.; Jones, A. T.; Dreher, Theo W.; Edwards, Michael C.; Gibbs, Adrian; Haenni, Anne Lise; Hammond, Rosemarie W.; Jupin, Isabelle; Sabanadzovic, Sead; Ghanem-Sabanadzovic, N. Abou; Agranovsky, Alexey A.; Bar‐Joseph, M.; Boscia, D.; Candresse, T.; Coutts, Robert H.A.; Dolja, Valerian V.; Gonsalves, D.; Hu, Junying; Wilhelm, Jochen; Minafra, A.; Namba, Susumu; Wisler, C.G.; Accotto, G. P.; Foster, Gary D.; Karasev, Alexander V.; Mawassi, Munir; Rowhani, Adib; Vishnichenko, V. K.; Wisler, G. C.; Завриев, С. К.; Wright, P.J.; Revill, Peter

doi:10.1016/b978-0-12-249951-7.50015-8

Cited by 6 publications

(1 citation statement)

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“…The bacteriophage MS2 is a small positive-sense single-stranded RNA (+ssRNA) virus from the family Leviviridae . − The MS2 genomic RNA is encapsulated by an icosahedral capsid, which is built from 178 copies of a coat protein (CP) and a single copy of a maturation protein. − The small size and simplicity of MS2 make it a good model system to study the assembly of icosahedral viruses. Moreover, MS2 and related phage capsids have been used for targeted drug delivery − and as scaffolds for antigen presentation of small epitopes in vaccine design. − These and other applications make MS2 capsid assembly an important system to study.…”

Section: Introductionmentioning

confidence: 99%

Understanding the Folding Mediated Assembly of the Bacteriophage MS2 Coat Protein Dimers

Prakash

Gosavi

2021

J. Phys. Chem. B

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The capsids of RNA viruses such as MS2 are great models for studying protein self-assembly because they are made almost entirely of multiple copies of a single coat protein (CP). Although CP is the minimal repeating unit of the capsid, previous studies have shown that CP exists as a homodimer (CP2) even in an acid-disassembled system, indicating that CP2 is an obligate dimer. Here, we investigate the molecular basis of this obligate dimerization using coarse-grained structure-based models and molecular dynamics simulations. We find that, unlike monomeric proteins of similar size, CP populates a single partially folded ensemble whose “foldedness” is sensitive to denaturing conditions. In contrast, CP2 folds similarly to single-domain proteins populating only the folded and the unfolded ensembles, separated by a prominent folding free energy barrier. Several intramonomer contacts form early, but the CP2 folding barrier is crossed only when the intermonomer contacts are made. A dissection of the structure of CP2 through mutant folding simulations shows that the folding barrier arises both from the topology of CP and the interface contacts of CP2. Together, our results show that CP2 is an obligate dimer because of kinetic stability, that is, dimerization induces a folding barrier and that makes it difficult for proteins in the dimer minimum to partially unfold and access the monomeric state without completely unfolding. We discuss the advantages of this obligate dimerization in the context of dimer design and virus stability.

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