Author

K. Grehan

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 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:host-pathogen & immune response· 3 Organism:mouse· 2 Organism:yeast· 2 Approach:biophysical modeling· 1 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

N. J. Stonehouse· 6 shared L. Sherry· 4 shared D. J. Rowlands· 3 shared D. Rowlands· 3 shared J. S. Snowden· 3 shared N. J. Kingston· 3 shared A. J. Macadam· 2 shared C. Porta· 2 shared

Activity by Year

2019-2024 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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6 shared papersMicrobiology

N. J. Stonehouse

Mutual co-authors in cluster

Author profile →

7 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

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

Protease-independent production of poliovirus virus-like particles in Pichia pastoris: Implications for efficient vaccine development and insights into capsid assembly.

L. Sherry, J. J. Swanson, K. Grehan, H. Xu, M. Uchida, I. M. Jones, N. J. Stonehouse, D. J. Rowlands

This study produces protease-independent poliovirus VLPs in Pichia pastoris, showing they maintain native antigenicity and thermostability, suggesting potential for improved vaccine development.

bioRxiv · Sep 16, 2022Microbiology

Production and characterisation of stabilised PV-3 virus-like particles using Pichia pastoris

L. Sherry, K. Grehan, J. J. Swanson, M. W. Bahar, C. Porta, E. E. Fry, D. I. Stuart, D. Rowlands, N. J. Stonehouse

This paper produces and characterizes stabilized PV-3 virus-like particles using Pichia pastoris, showing improved thermostability and antigen ratio compared to wild-type PV-3.

bioRxiv · Sep 16, 2022Microbiology

A conserved glutathione binding site in poliovirus is a target for antivirals and vaccine stabilisation

M. W. Bahar, V. Nasta, H. Fox, L. Sherry, K. Grehan, C. Porta, A. J. Macadam, N. J. Stonehouse, D. J. Rowlands, E. E. Fry, D. I. Stuart

This study identifies a conserved glutathione binding site in poliovirus VLPs that can be targeted by antivirals and used to stabilize vaccines.

bioRxiv · Sep 8, 2022Biochemistry

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

The bat influenza H17N10 can be neutralized by broadly-neutralizing monoclonal antibodies and its neuraminidase can facilitate viral egress.

G. Carnell, E. Giotis, K. Grehan, F. Ferrara, S. Mather, E. Molesti, S. Scott, A. Pessi, K. Lacek, N. Temperton

This paper shows that bat influenza H17N10 can be neutralized by human antibodies and its neuraminidase N10 aids viral release without using sialic acid as a receptor.

bioRxiv · Jan 12, 2019 · PreprintMicrobiology