Author

J. S. Snowden

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Microbiology· 4 Immunology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:mouse· 3 Assay:cryo-EM· 2 Research Focus:host-pathogen & immune response· 2 Approach:microscopy & imaging analysis· 2 Research Focus:protein structure prediction· 2 Approach:biophysical modeling· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

N. J. Stonehouse· 6 shared D. J. Rowlands· 3 shared K. Grehan· 3 shared N. A. Ranson· 3 shared N. J. Kingston· 3 shared D. Rowlands· 2 shared J. Alzahrani· 2 shared J. M. Hogle· 2 shared

Activity by Year

2019-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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6 shared papersMicrobiology

N. J. Stonehouse

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6 papers

Recent·Most cited

Mechanism of enterovirus VP0 maturation cleavage based on the structure of a stabilised assembly intermediate.

N. J. Kingston, J. S. Snowden, K. Grehan, P. K. Hall, E. V. Hietanen, T. C. Passchier, S. J. Polyak, D. J. Filman, J. M. Hogle, D. Rowlands, N. J. Stonehouse

The paper determines the molecular mechanism of VP0 cleavage in enteroviruses using structural and bioinformatic analysis of a provirion intermediate.

bioRxiv · Apr 6, 2024Microbiology

Amino acid substitutions in norovirus VP1 dictate cell tropism via an attachment process dependent on membrane mobility.

J. T. Mills, S. C. Minogue, J. S. Snowden, K. E. Carnahan, D. J. Rowlands, N. J. Stonehouse, C. E. Wobus, M. R. Herod

This study identifies an amino acid substitution in norovirus VP1 that enhances cellular attachment and alters tropism by affecting receptor recruitment and membrane mobility.

bioRxiv · Feb 17, 2023 · PreprintMicrobiology

Production of antigenically stable enterovirus A71 virus-like particles in Pichia pastoris as a vaccine candidate.

N. J. Kingston, J. S. Snowden, A. Martyna, M. Shegdar, K. Grehan, A. Tedcastle, E. Pegg, H. Fox, A. J. Macadam, J. Martin, J. M. Hogle, D. Rowlands, N. J. Stonehouse

This study produces antigenically stable EVA71 virus-like particles in Pichia pastoris, showing they retain native antigenic conformation and elicit neutralising antibodies comparable to inactivated virus vaccines.

bioRxiv · Jan 30, 2023 · PreprintImmunology

VelcroVax: a bolt-on vaccine platform technology improves antibody titres against a viral glycoprotein in mice

N. J. Stonehouse, N. J. Kingston, K. Grehan, J. S. Snowden, M. Hassall, J. Alzahrani, G. C. Paesen, L. Sherry, C. R. Hayward, A. Roe, S. Stephen, D. C. Tomlinson, A. Zeltina, K. J. Doores, N. A. Ranson, , D. J. Rowlands

VelcroVax is a vaccine platform that enhances antibody titres against a viral glycoprotein in mice by combining a modified VLP with a SUMO-tagged antigen.

bioRxiv · Apr 22, 2022 · PreprintImmunology

Structural insight into Pichia pastoris fatty acid synthase

J. S. Snowden, J. Alzahrani, L. Sherry, M. Stacey, D. J. Rowlands, N. A. Ranson, N. J. Stonehouse

The paper determines the structure of P. pastoris fatty acid synthase using cryoEM, identifying structural differences from S. cerevisiae FAS and resolving the mobile ACP domain.

bioRxiv · Jan 27, 2021Microbiology

High-Resolution Cryo-EM Reveals Dynamics in the Murine Norovirus Capsid

J. S. Snowden, D. L. Hurdiss, O. O. Adeyemi, N. A. Ranson, M. R. Herod, N. J. Stonehouse

This study uses cryo-EM to reveal the dynamic conformational changes in murine norovirus capsids, showing flexibility in protruding domains that impact virion stability and infectivity.

bioRxiv · Jul 4, 2019 · PreprintMicrobiology