Author

Y.-H. Wan

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· 4 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:host-pathogen & immune response· 4 Organism:human· 2 Assay:protein structure· 2 Research Focus:drug response / drug discovery· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

L. Stamatatos· 4 shared M. Pancera· 4 shared A. T. McGuire· 3 shared L. J. Homad· 3 shared A. B. Stuart· 2 shared A. McGuire· 2 shared D. Veesler· 2 shared J. Feng· 2 shared

Activity by Year

2020-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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4 shared papersImmunology

L. Stamatatos

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Immunization with a self-assembling nanoparticle vaccine displaying EBV gH/gL protects humanized mice against lethal viral challenge

H. Malhi, L. J. Homad, Y.-H. Wan, B. Poudel, B. Fiala, A. J. Borst, J. Y. Wang, C. Walkey, J. Price, A. Wall, S. Singh, Z. Moodie, S. Handa, C. Correnti, B. L. Stoddard, , A. McGuire

This study evaluates a nanoparticle vaccine displaying EBV gH/gL, showing it protects humanized mice against lethal EBV challenge, while monomeric gH/gL does not.

bioRxiv · Feb 17, 2022Immunology

Structural definition of a pan-sarbecovirus neutralizing epitope on the spike S2 subunit.

N. Hurlburt, L. Homad, I. Siha, M. F. Jenewein, A. MacCamy, Y.-H. Wan, J. Boonyaratanakornkit, A. M. Sholukh, P. Zhou, D. Burton, R. Andrabi, L. Stamatatos, M. Pancera, A. McGuire

This paper identifies a conserved neutralizing epitope on the spike S2 subunit of sarbecoviruses, demonstrating cross-neutralization against multiple variants and a bat coronavirus.

bioRxiv · Aug 2, 2021Immunology

Designed proteins assemble antibodies into modular nanocages

R. Divine, H. V. Dang, G. Ueda, J. A. Fallas, I. Vulovic, W. Sheffler, S. Saini, Y. T. Zhao, I. X. Raj, P. A. Morawski, M. F. Jennewein, L. J. Homad, Y.-H. Wan, M. R. Tooley, F. Seeger, , D. Baker

The paper designs modular nanocages that assemble antibodies into precise geometries, enhancing signaling and neutralization compared to free antibodies.

bioRxiv · Dec 1, 2020Biochemistry

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