Publications

Notable Recent Publications

These are some recent publications which give a flavour of the research from the Barclay lab. For a complete list of publications, please see below.

Species difference in ANP32A underlies influenza A virus polymerase host restriction. Nature (2016).
Jason S. Long, Efstathios S. Giotis, Olivier Moncorgé, Rebecca Frise, Bhakti Mistry, Joe James, Mireille Morisson, Munir Iqbal, Alain Vignal, Michael A. Skinner & Wendy S. Barclay

This paper identified a key factor that explained why the polymerases from avian influenza viruses are restricted in humans.  For more, please see the associated New and Views.

See our latest ANP32 papers here: eLIFE, Journal of Virology, Journal of Virology.

The mechanism of resistance to favipiravir in influenza. PNAS (2018).
Daniel H. Goldhill, Aartjan J. W. te Velthuis, Robert A. Fletcher, Pinky Langat, Maria Zambon, Angie Lackenby & Wendy S. Barclay

This paper showed how influenza could evolve resistance to favipiravir, an antiviral that may be used to treat influenza. The residue that mutated to give resistance was highly conserved suggesting that the mechanism of resistance may be applicable to other RNA viruses.

Internal genes of a highly pathogenic H5N1 influenza virus determine high viral replication in myeloid cells and severe outcome of infection in mice. Plos Path. (2018).
Hui Li*, Konrad C. Bradley*, Jason S. Long, Rebecca Frise, Jonathan W. Ashcroft, Lorian C. Hartgroves, Holly Shelton, Spyridon Makris, Cecilia Johansson, Bin Cao & Wendy S. Barclay

Why do avian influenza viruses like H5N1 cause such severe disease in humans? This paper demonstrated that H5N1 viruses replicate better than human viruses in myeloid cells from mice leading to a cytokine storm and more severe disease.

Citation

BibTex format

@unpublished{Peacock:2022:10.1101/2020.09.30.318311,
author = {Peacock, T and Goldhill, D and Zhou, J and Baillon, L and Frise, R and Swann, O and Kugathasan, R and Penn, R and Brown, J and Sanchez-David, R and Braga, L and Williamson, MK and Hassard, J and Staller, E and Hanley, B and Osborn, M and Giacca, M and Davidson, A and Matthews, D and Barclay, W},
doi = {10.1101/2020.09.30.318311},
publisher = {bioXriv},
title = {The furin cleavage site of SARS-CoV-2 spike protein is a key determinant for transmission due to enhanced replication in airway cells},
url = {http://dx.doi.org/10.1101/2020.09.30.318311},
year = {2022}
}
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RIS format (EndNote, RefMan)

TY  - UNPB
AB  - SARS-CoV-2 enters cells via its spike glycoprotein which must be cleaved sequentially at the S1/S2, then the S2’ cleavage sites (CS) to mediate membrane fusion. SARS-CoV-2 has a unique polybasic insertion at the S1/S2 CS, which we demonstrate can be cleaved by furin. Using lentiviral pseudotypes and a cell-culture adapted SARS-CoV-2 virus with a S1/S2 deletion, we show that the polybasic insertion is selected for in lung cells and primary human airway epithelial cultures but selected against in Vero E6, a cell line used for passaging SARS-CoV-2. We find this selective advantage depends on expression of the cell surface protease, TMPRSS2, that allows virus entry independent of endosomes thus avoiding antiviral IFITM proteins. SARS-CoV-2 virus lacking the S1/S2 furin CS was shed to lower titres from infected ferrets and was not transmitted to cohoused sentinel animals. Thus, the polybasic CS is a key determinant for efficient SARS-CoV-2 transmission.
AU  - Peacock,T
AU  - Goldhill,D
AU  - Zhou,J
AU  - Baillon,L
AU  - Frise,R
AU  - Swann,O
AU  - Kugathasan,R
AU  - Penn,R
AU  - Brown,J
AU  - Sanchez-David,R
AU  - Braga,L
AU  - Williamson,MK
AU  - Hassard,J
AU  - Staller,E
AU  - Hanley,B
AU  - Osborn,M
AU  - Giacca,M
AU  - Davidson,A
AU  - Matthews,D
AU  - Barclay,W
DO  - 10.1101/2020.09.30.318311
PB  - bioXriv
PY  - 2022///
TI  - The furin cleavage site of SARS-CoV-2 spike protein is a key determinant for transmission due to enhanced replication in airway cells
UR  - http://dx.doi.org/10.1101/2020.09.30.318311
UR  - https://www.biorxiv.org/content/10.1101/2020.09.30.318311v1
UR  - http://hdl.handle.net/10044/1/98542
ER  -
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