Author

A. B. Stuart

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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Immunology· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 3 Organism:human· 2 Assay:proteomics· 2 Assay:structural biology· 1

Frequent Co-Authors

J. Feng· 3 shared L. Stamatatos· 3 shared M. Pancera· 3 shared A. T. McGuire· 2 shared E. Seydoux· 2 shared J. A. Englund· 2 shared N. K. Hurlburt· 2 shared Y.-H. Wan· 2 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 41 mutual co-author links

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3 shared papersImmunology

J. Feng

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Author profile →

3 papers

Recent·Most cited

Isolation and Characterization of Cross-Neutralizing Coronavirus Antibodies from COVID-19+ Subjects

M. Jennewein, A. MacCamey, N. Akins, J. Feng, L. Homad, N. Hurlburt, E. Seydoux, Y.-H. Wang, A. B. Stuart, V. V. Edara, K. Floyd, A. Vanderheiden, J. R. Mascola, N. Doria-Rose, L. Wang, , L. Stamatatos

The paper isolates and characterizes cross-neutralizing antibodies from COVID-19 patients, identifying antibodies that neutralize both SARS-CoV-1 and SARS-CoV-2, including variants.

bioRxiv · Mar 23, 2021 · PreprintImmunology

Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation

N. K. Hurlburt, Y.-H. Wan, A. B. Stuart, J. Feng, A. T. McGuire, L. Stamatatos, M. Pancera

The paper determines the X-ray crystal structure of a potent SARS-CoV-2 neutralizing antibody, CV30, in complex with the RBD, showing its epitope overlaps with ACE2 binding site.

bioRxiv · Jun 12, 2020Immunology

Characterization of neutralizing antibodies from a SARS-CoV-2 infected individual

E. Seydoux, L. J. Homad, A. J. MacCamy, K. R. Parks, N. K. Hurlburt, M. F. Jennewein, N. R. Akins, A. B. Stuart, Y.-H. Wan, J. Feng, R. Nelson, S. Singh, K. W. Cohen, J. M. McElrath, J. A. Englund, , L. Stamatatos

This study characterizes neutralizing antibodies from a SARS-CoV-2 infected individual, finding that most antibodies are non-neutralizing and target epitopes outside the RBD, while two potent neutralizers bind the RBD with minimal mutation.

bioRxiv · May 12, 2020 · PreprintImmunology