In this section
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).
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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.
@article{Brown:2019:10.1099/jgv.0.001348,
author = {Brown, JC and Barclay, WS and Galiano, M and Harvey, R},
doi = {10.1099/jgv.0.001348},
journal = {Journal of General Virology},
pages = {456--466},
title = {Passage of influenza A/H3N2 viruses in human airway cells removes artefactual variants associated with neuraminidase-mediated binding.},
url = {http://dx.doi.org/10.1099/jgv.0.001348},
volume = {101},
year = {2019}
}
TY - JOUR
AB - Serological assays with modern influenza A/H3N2 viruses have become problematic due to the progressive reduction in the ability of viruses of this subtype to bind and agglutinate red blood cells (RBCs). This is due to reduced ability of the viral haemagglutinin (HA) glycoprotein to bind to the sialic acid-containing receptors presented by these cells. Additionally, as a result of reduced HA-mediated binding in cell culture, modern A/H3N2 viruses often acquire compensatory mutations during propagation that enable binding of cellular receptors through their neuraminidase (NA) surface protein. Viruses that have acquired this NA-mediated binding agglutinate RBCs through their NA, confusing the results of serological assays designed to assess HA antigenicity. Here we confirm with a large dataset that the acquisition of mutations that confer NA binding of RBCs is a culture artefact, and demonstrate that modern A/H3N2 isolates with acquired NA-binding mutations revert to a clinical-like NA sequence after a single passage in human airway epithelial (HAE) cells.
AU - Brown,JC
AU - Barclay,WS
AU - Galiano,M
AU - Harvey,R
DO - 10.1099/jgv.0.001348
EP - 466
PY - 2019///
SN - 0022-1317
SP - 456
TI - Passage of influenza A/H3N2 viruses in human airway cells removes artefactual variants associated with neuraminidase-mediated binding.
T2 - Journal of General Virology
UR - http://dx.doi.org/10.1099/jgv.0.001348
UR - https://www.ncbi.nlm.nih.gov/pubmed/31702542
UR - https://www.microbiologyresearch.org/content/journal/jgv/10.1099/jgv.0.001348
UR - http://hdl.handle.net/10044/1/74959
VL - 101
ER -
For any enquiries related to this group, please contact:
Professor Wendy Barclay
Chair in Influenza Virology
+44 (020) 7594 5035
w.barclay@imperial.ac.uk