Dr Toby Tuthill

Real name:

Group Leader

Molecular Biology, Structural biology, Virology

Toby Tuthill is a virologist interested in the molecular mechanisms used by viruses in the picornavirus family. Current areas of interest include cell entry, replication, assembly, structure, antigenicity and evolution. Research is intended to improve our understanding of the biology of these viruses and to apply this knowledge towards improved control of disease.

Toby joined The Pirbright Institute as a Research Fellow in 2009 after ten years postdoctoral experience in the laboratory of Professor Dave Rowlands at the University of Leeds.

News
Publications

Pirbright scientists investigate pig coronavirus infection to understand COVID-19 in humans

Early animal studies by Pirbright and Oxford yield promising results for new potential COVID-19 vaccine

Studies at Pirbright demonstrate two doses of Oxford University’s COVID-19 vaccine boosts immune response in pigs

Pirbright develops universal foot-and-mouth disease virus test

Pirbright begins testing new coronavirus vaccines on animals to help combat COVID-19

Swatek K N, Aumayr M, Pruneda J N, Visser L J, Berryman S, Kueck A F, Geurink P P, Ovaa H, van Kuppeveld F J M, Tuthill T J, Skern T, Komander D (2018)

Irreversible inactivation of ISG15 by a viral leader protease enables alternative infection detection strategies

Proceedings of the National Academy of Sciences of the United States of America 115 (10) , 2371-2376

Publisher’s version: https://doi.org/10.1073/pnas.1710617115

Newman J, Asfor A S, Berryman S, Jackson T, Curry S, Tuthill T J (2017)

The cellular chaperone heat shock protein 90 is required for foot-and-mouth disease virus capsid precursor processing and assembly of capsid pentamers

Journal of Virology 92 (5) , e01415-01417

Publisher’s version: http://dx.doi.org/10.1128/jvi.01415-17

Logan G, Newman J, Wright C F, Lasecka-Dykes L, Haydon D T, Cottam E M, Tuthill T J (2017)

Deep sequencing of foot-and-mouth disease virus reveals RNA sequences involved in genome packaging

Journal of Virology 92 (1) , e01159-01117

Publisher’s version: http://dx.doi.org/10.1128/JVI.01159-17

Herod M R, Gold S, Lasecka-Dykes L, Wright C, Ward J C, McLean T C, Forrest S, Jackson T, Tuthill T J, Rowlands D J, Stonehouse N J (2017)

Genetic economy in picornaviruses: foot-and-mouth disease virus replication exploits alternative precursor cleavage pathways

PLoS Pathogens 13 (10) , e1006666

Publisher’s version: http://dx.doi.org/10.1371/journal.ppat.1006666

Malik N, Kotecha A, Gold S, Asfor A, Ren J, Huiskonen J T, Tuthill T J, Fry E E, Stuart D I (2017)

Structures of foot and mouth disease virus pentamers: Insight into capsid dissociation and unexpected pentamer reassociation

PLOS Pathogens 13 (9) , e1006607

Publisher’s version: https://doi.org/10.1371/journal.ppat.1006607

Zhu L, Wang X, Ren J, Kotecha A, Walter T S, Yuan S, Yamashita T, Tuthill T J, Fry E E, Rao Z, Stuart D I (2016)

Groups

Picornavirus Molecular Biology

Dr Toby Tuthill

Pirbright scientists investigate pig coronavirus infection to understand COVID-19 in humans

Early animal studies by Pirbright and Oxford yield promising results for new potential COVID-19 vaccine

Studies at Pirbright demonstrate two doses of Oxford University’s COVID-19 vaccine boosts immune response in pigs

Pirbright develops universal foot-and-mouth disease virus test

Pirbright begins testing new coronavirus vaccines on animals to help combat COVID-19

Irreversible inactivation of ISG15 by a viral leader protease enables alternative infection detection strategies

The cellular chaperone heat shock protein 90 is required for foot-and-mouth disease virus capsid precursor processing and assembly of capsid pentamers

Deep sequencing of foot-and-mouth disease virus reveals RNA sequences involved in genome packaging

Genetic economy in picornaviruses: foot-and-mouth disease virus replication exploits alternative precursor cleavage pathways

Structures of foot and mouth disease virus pentamers: Insight into capsid dissociation and unexpected pentamer reassociation

Structure of human Aichi virus and implications for receptor binding

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