Author

E. Staller

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· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:host-pathogen & immune response· 5 Organism:human· 3 Research Focus:cell type annotation· 2 Organism:chicken / avian· 1 Approach:genetic perturbation / CRISPR· 1 Organism:mouse· 1 Organism:plant (other)· 1

Frequent Co-Authors

W. S. Barclay· 5 shared T. P. Peacock· 4 shared D. H. Goldhill· 3 shared J. S. Long· 3 shared O. C. Swann· 3 shared R. Frise· 3 shared C. M. Sheppard· 2 shared L. Baillon· 2 shared

Activity by Year

2019-2020 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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5 shared papersMicrobiology

W. S. Barclay

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5 papers

Recent·Most cited

The furin cleavage site of SARS-CoV-2 spike protein is a key determinant for transmission due to enhanced replication in airway cells.

T. P. Peacock, D. H. Goldhill, J. Zhou, L. Baillon, R. Frise, O. C. Swann, R. Kugathasan, R. Penn, J. C. Brown, R. Y. Sanchez-David, L. Braga, M. K. Williamson, J. A. Hassard, E. Staller, B. Hanley, , W. S. Barclay

This study shows the furin cleavage site in SARS-CoV-2 spike protein enhances replication in airway cells, contributing to transmission efficiency.

bioRxiv · Sep 30, 2020 · PreprintMicrobiology

Mammalian ANP32A and ANP32B proteins drive alternative avian influenza virus polymerase adaptations

T. P. Peacock, C. M. Sheppard, E. Staller, R. Frise, O. C. Swann, D. Goldhill, J. S. Long, W. S. Barclay

This study identifies alternative PB2 adaptations that enable influenza polymerase to use mammalian ANP32 proteins, with PB2-E627K showing a preference for ANP32B.

bioRxiv · Sep 3, 2020 · PreprintMicrobiology

Swine ANP32A supports avian influenza virus polymerase

T. P. Peacock, O. C. Swann, E. Staller, P. B. Leung, D. H. Goldhill, H. Zhou, J. S. Long, W. S. Barclay

This study shows swine ANP32A supports avian influenza polymerase activity, and human-adapted viruses evolved to use human ANP32 proteins more efficiently.

Journal of Virology · Jun 1, 2020Peer-reviewedMicrobiology

A rare variant in ANP32B impairs influenza virus replication in human cells

E. Staller, L. Baillon, R. Frise, T. P. Peacock, C. M. Sheppard, V. Sancho-Shimizu, W. S. Barclay

This study identifies a rare variant in ANP32B that impairs influenza virus replication by disrupting FluPol dimer formation and function.

bioRxiv · Apr 6, 2020Microbiology

Avian ANP32B does not support influenza A virus polymerase and influenza A virus relies exclusively on ANP32A in chicken cells.

J. S. Long, A. Idoko-Akoh, B. Mistry, D. H. Goldhill, E. Staller, J. Schreyer, C. Ross, S. Goodbourn, H. Shelton, M. A. Skinner, H. M. Sang, M. J. McGrew, W. S. Barclay

bioRxiv · Jan 4, 2019 · PreprintMicrobiology