Author

G. E. Seabright

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· 1 Immunology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Assay:structural biology· 2 Research Focus:drug response / drug discovery· 1 Approach:genetic perturbation / CRISPR· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

J. D. Allen· 3 shared M. Crispin· 3 shared A. B. Ward· 2 shared M. J. van Gils· 2 shared R. W. Sanders· 2 shared Y. Watanabe· 2 shared A. Antanasijevic· 1 shared A. D'addabbo· 1 shared

Activity by Year

2020-2020 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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3 shared papersBiochemistry

J. D. Allen

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Enhancing glycan occupancy of soluble HIV-1 envelope trimers to mimic the native viral spike

R. Derking, J. D. Allen, C. Cottrell, K. Sliepen, G. E. Seabright, W.-H. Lee, K. Rantalainen, A. Antanasijevic, J. Copps, A. Yasmeen, P. van der Woude, S. W. de Taeye, T. L. G. M. van den Kerkhof, P. J. Klasse, G. Ozorowski, , R. W. Sanders

The paper modifies HIV-1 Env trimers to increase glycan occupancy and reduce artificial glycan holes, improving vaccine antigen design.

bioRxiv · Jul 2, 2020Biochemistry

Networks of HIV-1 envelope glycans maintain antibody epitopes in the face of glycan additions and deletions

G. E. Seabright, C. A. Cottrell, M. J. van Gils, A. D'addabbo, D. J. Harvey, A.-J. Beherns, J. D. Allen, Y. Watanabe, A. Maker, S. Vasiljevic, N. de Val, R. W. Sanders, A. B. Ward, M. Crispin

The paper investigates how HIV-1 envelope glycan networks affect the formation and stability of broadly neutralizing antibody epitopes, showing their importance in immunogen design.

bioRxiv · Feb 21, 2020Immunology

Vulnerabilities in coronavirus glycan shields despite extensive glycosylation

Y. Watanabe, Z. T. Berndsen, J. Raghwani, G. E. Seabright, J. D. Allen, J. S. McLellan, I. A. Wilson, T. A. Bowden, A. B. Ward, M. Crispin

This study identifies vulnerabilities in coronavirus glycan shields by showing that MERS S protein has under-processed oligomannose-type glycan clusters, unlike SARS and HKU1 CoVs, and that these glycans do not form an effective shield against antibodies.

bioRxiv · Feb 20, 2020Microbiology