Author

M. Kavanagh Williamson

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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Biochemistry· 2 Cell Biology· 2 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:host-pathogen & immune response· 4 Organism:human· 4 Research Focus:cell type annotation· 2 Research Focus:drug response / drug discovery· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:clustering· 1 Research Focus:differential expression· 1

Frequent Co-Authors

A. D. Davidson· 5 shared D. A. Matthews· 3 shared I. Berger· 3 shared K. Gupta· 3 shared C. Schaffitzel· 2 shared D. Buzas· 2 shared F. Garzoni· 2 shared J. A. Hiscox· 2 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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Curved chords = mutual co-authorship

5 shared papersMicrobiology

A. D. Davidson

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

Antibodies generated in vitro and in vivo elucidate design of a thermostable ADDomer COVID-19 nasal nanoparticle vaccine

D. Buzas, H. A. Bunzel, O. Staufer, E. Milodowski, G. Edmonds, J. Bufton, B. Vidana Matteo, S. Yadav, K. Gupta, C. Fletcher, M. Kavanagh Williamson, A. Harrison, U. Borucu, J. Capin, O. Francis, , I. Berger

This study develops a thermostable ADDomer-based nanoparticle vaccine that neutralizes SARS-CoV-2 and cross-reacts with VOCs, demonstrating its potential for nasal administration.

bioRxiv · Mar 17, 2023Biochemistry

Development of SARS-CoV-2 replicons for the ancestral virus and variant of concern Delta for antiviral screening.

M. Erdmann, M. Kavanagh Williamson, T. Jearanaiwitayakul, J. Bazire, D. A. Matthews, A. D. Davidson

The paper develops SARS-CoV-2 replicons for the ancestral virus and Delta variant to screen antiviral compounds, showing sensitivity to remdesivir.

bioRxiv · Oct 11, 2022Microbiology

The Free Fatty Acid-Binding Pocket is a Conserved Hallmark in Pathogenic β-Coronavirus Spike Proteins from SARS-CoV to Omicron

C. Toelzer, K. Gupta, S. K. N. Yadav, L. Hodgson, M. Kavanagh Williamson, D. Buzas, U. Borucu, K. Powers, R. Stenner, K. Vasileiou, F. Garzoni, D. Fitzgerald, C. Payre, G. Lambeau, A. D. Davidson, , C. Schaffitzel

The paper identifies a conserved free fatty acid-binding pocket in pathogenic β-coronavirus spike proteins that suppresses viral infection and replication.

bioRxiv · Apr 22, 2022Biochemistry

The SARS-CoV-2 Spike protein disrupts human cardiac pericytes function through CD147-receptor-mediated signalling: a potential non-infective mechanism of COVID-19 microvascular disease

E. Avolio, M. Carrabba, R. Milligan, M. Kavanagh Williamson, A. P. Beltrami, K. Gupta, K. T. Elvers, M. Gamez, R. Foster, K. Gillespie, F. Hamilton, D. Arnold, I. Berger, M. Caputo, A. D. Davidson, , P. Madeddu

This paper shows that SARS-CoV-2 Spike protein causes cardiac pericyte dysfunction through CD147-mediated signaling, without infecting the cells.

bioRxiv · Dec 21, 2020Cell Biology

Sequential infection with influenza A virus followed by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) leads to more severe disease and encephalitis in a mouse model of COVID-19.

J. J. Clark, R. Penrice-Randal, P. Sharma, A. Kipar, X. Dong, S. Pennington, A. E. Marriott, S. Colombo, A. D. Davidson, M. Kavanagh Williamson, D. A. Matthews, L. Turtle, T. Prince, G. Hughes, E. I. Patterson, , J. P. Stewart

This study shows that sequential infection with influenza A virus followed by SARS-CoV-2 in mice leads to more severe disease and encephalitis compared to single infections.

bioRxiv · Oct 13, 2020 · PreprintMicrobiology

Neuropilin-1 is a host factor for SARS-CoV-2 infection

J. L. Daly, B. Simonetti, C. Anton Plagaro, M. Kavanagh Williamson, D. K. Shoemark, L. Simon-Gracia, K. Klein, M. Bauer, R. Hollandi, U. F. Greber, P. Horvath, R. B. Sessions, A. Helenius, J. A. Hiscox, T. Teesalu, , Y. Yamauchi

This study shows that SARS-CoV-2's S1 protein binds to NRP1 via the CendR motif, enhancing infection and identifying NRP1 as a therapeutic target.

bioRxiv · Jun 5, 2020Cell Biology