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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Curved chords = mutual co-authorship

3 shared papersBiochemistry

J. D. Allen

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivJul 2, 2020

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

R. Derking, J. D. Allen, C. Cottrell…·R. W. Sanders

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

DOI 10.1016/j.celrep.2021.108933

proteomicsgenetic perturbation / CRISPR

𝕏 PostBluesky

ImmunologybioRxivFeb 21, 2020

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…·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.

DOI 10.1016/j.str.2020.04.022

structural biologyexperimental assay

𝕏 PostBluesky

MicrobiologybioRxivFeb 20, 2020

Vulnerabilities in coronavirus glycan shields despite extensive glycosylation

Y. Watanabe, Z. T. Berndsen, J. Raghwani…·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.

DOI 10.1038/s41467-020-16567-0

structural biologyexperimental assay

𝕏 PostBluesky