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Phosphorylation of Single Stranded RNA Virus Proteins and Potential for Novel Therapeutic Strategies.

Keck F, Ataey P, Amaya M, Bailey C, Narayanan A.

Viruses. 2015 Oct 12;7(10):5257-73. doi: 10.3390/v7102872. Review.


New tags for recombinant protein detection and O-glycosylation reporters.

Petris G, Bestagno M, Arnoldi F, Burrone OR.

PLoS One. 2014 May 6;9(5):e96700. doi: 10.1371/journal.pone.0096700.


Rotavirus increases levels of lipidated LC3 supporting accumulation of infectious progeny virus without inducing autophagosome formation.

Arnoldi F, De Lorenzo G, Mano M, Schraner EM, Wild P, Eichwald C, Burrone OR.

PLoS One. 2014 Apr 15;9(4):e95197. doi: 10.1371/journal.pone.0095197.


A novel form of rotavirus NSP2 and phosphorylation-dependent NSP2-NSP5 interactions are associated with viroplasm assembly.

Criglar JM, Hu L, Crawford SE, Hyser JM, Broughman JR, Prasad BV, Estes MK.

J Virol. 2014 Jan;88(2):786-98. doi: 10.1128/JVI.03022-13.


Thiazolides, a new class of antiviral agents effective against rotavirus infection, target viral morphogenesis, inhibiting viroplasm formation.

La Frazia S, Ciucci A, Arnoldi F, Coira M, Gianferretti P, Angelini M, Belardo G, Burrone OR, Rossignol JF, Santoro MG.

J Virol. 2013 Oct;87(20):11096-106. doi: 10.1128/JVI.01213-13.


Rotavirus viroplasm proteins interact with the cellular SUMOylation system: implications for viroplasm-like structure formation.

Campagna M, Marcos-Villar L, Arnoldi F, de la Cruz-Herrera CF, Gallego P, González-Santamaría J, González D, Lopitz-Otsoa F, Rodriguez MS, Burrone OR, Rivas C.

J Virol. 2013 Jan;87(2):807-17. doi: 10.1128/JVI.01578-12.


Rotavirus non-structural proteins: structure and function.

Hu L, Crawford SE, Hyser JM, Estes MK, Prasad BV.

Curr Opin Virol. 2012 Aug;2(4):380-8. doi: 10.1016/j.coviro.2012.06.003. Review.


Rotavirus replication requires a functional proteasome for effective assembly of viroplasms.

Contin R, Arnoldi F, Mano M, Burrone OR.

J Virol. 2011 Mar;85(6):2781-92. doi: 10.1128/JVI.01631-10.


Assortment and packaging of the segmented rotavirus genome.

McDonald SM, Patton JT.

Trends Microbiol. 2011 Mar;19(3):136-44. doi: 10.1016/j.tim.2010.12.002. Review.


Rotaviruses associate with cellular lipid droplet components to replicate in viroplasms, and compounds disrupting or blocking lipid droplets inhibit viroplasm formation and viral replication.

Cheung W, Gill M, Esposito A, Kaminski CF, Courousse N, Chwetzoff S, Trugnan G, Keshavan N, Lever A, Desselberger U.

J Virol. 2010 Jul;84(13):6782-98. doi: 10.1128/JVI.01757-09.


Sequestration of free tubulin molecules by the viral protein NSP2 induces microtubule depolymerization during rotavirus infection.

Martin D, Duarte M, Lepault J, Poncet D.

J Virol. 2010 Mar;84(5):2522-32. doi: 10.1128/JVI.01883-09.


In vivo site-specific biotinylation of proteins within the secretory pathway using a single vector system.

Predonzani A, Arnoldi F, López-Requena A, Burrone OR.

BMC Biotechnol. 2008 Apr 18;8:41. doi: 10.1186/1472-6750-8-41.


An ATPase activity associated with the rotavirus phosphoprotein NSP5.

Bar-Magen T, Spencer E, Patton JT.

Virology. 2007 Dec 20;369(2):389-99.


Crystallographic and biochemical analysis of rotavirus NSP2 with nucleotides reveals a nucleoside diphosphate kinase-like activity.

Kumar M, Jayaram H, Vasquez-Del Carpio R, Jiang X, Taraporewala ZF, Jacobson RH, Patton JT, Prasad BV.

J Virol. 2007 Nov;81(22):12272-84.


Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2.

Arnoldi F, Campagna M, Eichwald C, Desselberger U, Burrone OR.

J Virol. 2007 Mar;81(5):2128-37.


Fusion of tags induces spurious phosphorylation of rotavirus NSP5.

Campagna M, Burrone OR.

J Virol. 2006 Aug;80(16):8283-4; author reply 8284-5. No abstract available.


Uncoupling substrate and activation functions of rotavirus NSP5: phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation.

Eichwald C, Jacob G, Muszynski B, Allende JE, Burrone OR.

Proc Natl Acad Sci U S A. 2004 Nov 16;101(46):16304-9.

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