Publications 2019-2024
2024
– Chenavier F, Zarkadas E, Freslon LL, Stelfox AJ, Schoehn G, Ruigrok RWH, Ballandras-Colas A and Crépin T (2024) Influenza A virus antiparallel helical nucleocapsid-like pseudo-atomic structure. Nucleic Acids Res : gkae1211. https://doi.org/10.1093/nar/gkae1211.
– Bessonne M, Morel J, Nevers Q, Da Costa B, Ballandras-Colas A, Chenavier F, Grange M, Roussel A, Crépin T and Delmas B (2024) Antiviral activity of intracellular nanobodies targeting the influenza virus RNA-polymerase core. PLoS Pathog, 20(6):e1011642. https://doi.org/10.1371/journal.ppat.1011642.
– Burmeister WP, Boutin L, Balestra AC, Gröger H, Ballandras-Colas A, Hutin S, Kraft C, Grimm C, Böttcher B, Fischer U, Tarbouriech N, Iseni F. (2024) Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus. PLoS Pathog, 20(5):e1011652. https://doi.org/10.1371/journal.ppat.1011652.
– Quignon E, Ferhadian D, Hache A, Vivet-Boudou V, Isel C, Printz-Schweigert A, Donchet A, Crépin T and Marquet R (2024) Structural impact of the interaction of the influenza A virus nucleoprotein with genomic RNA segments. Viruses, 16(3):421. https://doi.org/10.3390/v16030421.
2023
– Chenavier F, Estrozi LF, Teulon J-M, Zarkadas E, Freslon LL, Pellequer J-L, Ruigrok RWH, Schoehn G, Ballandras-Colas A and Crépin T (2023) Cryo-EM structure of influenza helical nucleocapsid reveals NP-NP and NP-RNA interactions as a model for the genome encapsidation. Sci Adv, 9(50):eadj9974. https://doi.org/10.1126/sciadv.adj9974.
– Camacho-Zarco A, Yu L, Krischuns T, Dedeoglu S, Maurin D, Bouvignies G, Crépin T, Ruigrok RWH, Cusack S, Naffakh N and Blackledge M (2023) Multivalent dynamic colocalization of avian influenza polymerase and nucleoprotein by intrinsically disordered ANP32A reveals the molecular basis of human adaptation. J Am Chem Soc, 145(38):20985-21001. https://doi.org/10.1021/jacs.3c06965.
– Schoehn G, Chenavier F and Crépin T (2023) Advances in Structural Virology via Cryo-EM in 2022. Viruses, 15(6), 1315 ; https://doi.org/10.3390/v15061315 (Editorial).
– Guseva S, Schnapka V, Adamski W, Maurin D, Ruigrok RWH, Salvi N and Blackledge M (2023) Liquid−liquid phase separation modifies the dynamic properties of intrinsically disordered proteins. J Am Chem Soc, 145, 10548–10563. doi : doi.org/10.1021/jacs.2c13647.
2022
– Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E and Crépin T (2022) Borna disease virus 1 phosphoprotein forms a tetramer and interacts with host factors involved in DNA double-strand break repair and mRNA processing. Viruses, 14(11), 2358 ; https://doi.org/10.3390/ v14112358.
– Guillon A, Brea-Diakite D, Cezard A, Wacquiez A, Baranek T, Bourgeais J, Picou F, Vasseur V, Meyer L, Chevalier C, Auvet A, Carballido JM, Nadal Desbarats L, Dingli F, Turtoi A, Le Gouellec A, Fauvelle F, Donchet A, Crépin T, Hiemstra PS, Paget C, Loew D, Herault O, Naffakh N, Le Goffic R and Si-Tahar M (2022) Host succinate inhibits influenza virus infection through succinylation and nuclear retention of the viral nucleoprotein. EMBO J, e108306. https://doi.org/10.15252/embj.2021108306.
– Jóźwik IK, Li W, Zhang DW, Wong D, Grawenhoff J, Ballandras-Colas A, Aiyer S, Cherepanov P, Engelman AN, Lyumkis D (2022) B-to-A transition in target DNA during retroviral integration. Nucleic Acids Res, 50(15):8898-8918. https://doi.org/10.1093/nar/gkac644.
– Ballandras-Colas A, Chivukula V, Gruszka DT, Shan Z, Singh PK, Pye VE, McLean RK, Bedwell GJ, Li W, Nans A, Cook NJ, Fadel HJ, Poeschla EM, Griffiths DJ, Vargas J, Taylor IA, Lyumkis D, Yardimci H, Engelman AN, Cherepanov P (2022) Multivalent interactions essential for lentiviral integrase function. Nat Commun, 13(1):2416. https://doi.org/10.1038/s41467-022-29928-8.
– Bessa LM, Guseva S, Camacho-Zarco AR, Salvi N, Maurin D, Perez LM, Botova M, Malki A, Nanao M, Jensen MR, Ruigrok RWH and Blackledge M (2022) The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex with its viral partner nsp3a. Sci Adv, 8, eabm4034. https://doi.org/10.1126/ sciadv.abm4034.
– Ruigrok RWH, Drouet E, Morand P and Tarbouriech N (2022). Virus humains anciens, récents et zoonotiques : une histoire sans fin ? Virologie, 26 (3), 219-221. https://doi.org/10.1684/vir.2022.0957 (Review).
2021
– Kolakofsky D, Le Mercier P, Nishio M, Blackledge M, Crépin T and Ruigrok RWH (2021) Sendai virus and a unified model of Mononegavirus RNA synthesis. Viruses, 13(12):2466. https://doi.org/10.3390/v13122466 (Review).
– Terrier O, Si-Tahar M, Ducatez M, Chevalier C, Pizzorno A, Le Goffic R, Crépin T, Simon G and Naffakh N (2021) Influenza viruses and coronaviruses : knowns, unknowns, and common research challenges. PLoS Pathog, 17(12):e1010106. https://doi.org/10.1371/journal.ppat.1010106 (Review).
2020
– Donchet A, Vassal-Stermann E, Gérard FCA, Ruigrok RWH and Crépin T (2020) Differential behaviours and preferential bindings of influenza nucleoproteins on importins-α. Viruses, 12, 834. doi:10.3390/v12080834.
– Swale C, Da Costa B, Sedano L, Garzoni F, McCarthy AA, Berger I, Bieniossek C, Ruigrok RWH, Delmas B and Crépin T (2020) X-ray structure of the human karyopherin RanBP5, an essential factor for influenza polymerase nuclear trafficking. J Mol Biol, 432(10):3353-3359. https://doi.org/10.1016/j.jmb.2020. 03.021.
– Guseva S, Milles S, Jensen MR, Salvi N, Kleman J-P, Maurin D, Ruigrok RWH and Blackledge M (2020) Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. Sci Adv 6 : eaaz7095. https://doi.org/10.1126/sciadv.aaz7095.
– Guseva S, Milles S, Jensen MR, Schoehn G, Ruigrok RWH and Blackledge M (2020) Structure, dynamics and phase separation of measles virus RNA replication machinery. Curr Opin Virol, 41:59–67. https://doi.org/10.1016/j.coviro.2020.05.006 (Review).
2019
– Ashraf U, Tengo L, Le Corre L, Fournier G, Busca P, McCarthy AA, Rameix-Welti M-A, Gravier-Pelletier C, Ruigrok RW, Jacob Y, Vidalain P-O, Pietrancosta N, Crépin T and Naffakh N (2019) Destabilisation of the human RED-SMU1 splicing complex as a basis for host-directed anti-influenza strategy. Proc Natl Acad Sci USA, 116:10968-10977. https://doi.org/10.1073/pnas.1901214116.
– Donchet A, Oliva J, Labaronne A, Tengo L, Miloudi M, Gérard FCA, Mas C, Schoehn G, Ruigrok RW, Ducatez M and Crépin T (2019) The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NPCORE, with or without a NPTAIL for nuclear transport. Sci Rep, 9:600. https://doi.org/10.1038/s41598-018-37306-y.
– Desfosses A, Milles S, Jensen MR, Guseva S, Colletier J-P, Maurin D, Schoehn G, Gutsche I, Ruigrok RWH and Blackledge M (2019) Assembly and cryo-EM structures of RNA-specific measles virus nucleocapsids provide mechanistic insight into paramyxoviral replication. Proc Natl Acad Sci USA 116:4256-4264. https://doi.org/10.1073/pnas.1816417116.
– Guseva S, Milles S, Blackledge M and Ruigrok RWH (2019). The nucleoprotein and phosphoprotein of measles virus. Front Microbiol : 10:1832. https://doi.org/10.3389/fmicb.2019.01832 (Review).
Representative publications
– Chenavier F, Zarkadas E, Freslon LL, Stelfox AJ, Schoehn G, Ruigrok RWH, Ballandras-Colas A and Crépin T (2024) Influenza A virus antiparallel helical nucleocapsid-like pseudo-atomic structure. Nucleic Acids Res : gkae1211. https://doi.org/10.1093/nar/gkae1211.
– Guseva S, Milles S, Jensen MR, Salvi N, Kleman J-P, Maurin D, Ruigrok RWH and Blackledge M (2020) Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. Sci Adv 6 : eaaz7095. https://doi.org/10.1126/sciadv.aaz7095.
– Gutsche I, Desfosses A, Effantin G, Ling WL, Haupt M, Ruigrok RWH, Sachse C and Schoehn G (2015) Near-atomic cryo-EM structure of the helical Measles virus nucleocapsid. Science 348 : 704-707. https://doi.org/10.1126/science.aaa5137.
– Reich S, Guilligay D, Pflug A, Malet H, Berger I, Crépin T, Hart D, Lunardi T, Nanao M, Ruigrok RW, Cusack S (2014) Structural insight into cap-snatching and RNA synthesis by influenza polymerase. Nature 516 : 361-6. https://doi.org/10.1038/nature14009.
– Chenavas S, Estrozi LF, Slama-Schwok A, Delmas B, Di Primo C, Baudin F, Li X, Crépin T and Ruigrok RW (2013) Monomeric nucleoprotein of influenza A virus. PLoS Pathog 9 : e1003275. https://doi.org/10.1371/journal. ppat.1003275.
– Ruigrok RWH, Crépin T and Kolakofsky D (2011) Nucleoproteins and nucleocapsids of negative-strand RNA viruses. Curr Opin Microbiol 14 : 504–510. https://doi.org/10.1016/j.mib.2011.07.011 (Review).
– Jensen MR, Communie G, Ribeiro EA, Martinez N, Desfosses A, Salmon L, Jamin M, Mollica L, Gabel F, Longhi S, Ruigrok RWH and Blackledge M (2011) Intrinsic disorder in intact measles virus nucleocapsids. Proc Natl Acad Sci USA 108 : 9839-9844. https://doi.org/10.1073/pnas.1103270108.
– Dias A, Bouvier D, Crépin T, McCarthy AA, Hart DJ, Baudin F, Cusack S and Ruigrok RW (2009) The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit. Nature 458 : 914-918. https://doi.org/10.1038/nature07745.
– Albertini AAV, Wernimont AK, Muziol T, Ravelli RBG, Clapier CR, Schoehn G, Weissenhorn W and Ruigrok RWH (2006) Crystal structure of the rabies virus nucleoprotein-RNA complex. Science 313 : 357-360. https://doi.org/10.1126/science.1125280.
– Tarbouriech N, Curran J, Ruigrok RWH and Burmeister WP (2000). Tetrameric coiled coil domain of Sendai virus phosphoprotein. Nat Struct Biol 7 : 777-781. https://doi.org/10.1038/79013.
– Klumpp K, Ruigrok RWH and Baudin F (1997) Roles of the influenza virus polymerase and nucleoprotein in forming a functional RNP structure. EMBO J 16 : 1248-1257. https://doi.org/10.1093/emboj/16.6.1248.
– Burmeister WP, Ruigrok RWH and Cusack S (1992) The 2.2 Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. EMBO J 11 : 49-56. https://doi.org/10.1002/j.1460-2075.1992.tb05026.x.