Author

N. K. Hurlburt

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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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 4 Organism:human· 3 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Organism:plant (other)· 1 Assay:structural biology· 1

Frequent Co-Authors

M. Pancera· 4 shared A. B. Stuart· 2 shared A. T. McGuire· 2 shared J. Feng· 2 shared L. Stamatatos· 2 shared Y.-H. Wan· 2 shared A. B. Ward· 1 shared A. H. Idris· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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4 shared papersImmunology

M. Pancera

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4 papers

Recent·Most cited

Broadly inhibitory antibodies against severe malaria virulence proteins

R. A. Reyes, S. S. R. Raghavan, N. K. Hurlburt, V. Introini, I. H. Kana, R. W. Jensen, E. Martinez-Scholze, M. Gestal-Mato, C. B. Bau, M. L. Fernandez-Quintero, J. R. Loeffler, J. A. Ferguson, W.-H. Lee, G. M. Martin, T. G. Theander, , T. Lavstsen

The paper identifies two human monoclonal antibodies that broadly inhibit PfEMP1's binding to EPCR, a key process in severe malaria pathogenesis.

bioRxiv · Jan 25, 2024Immunology

The light chain of the L9 antibody is critical for binding circumsporozoite protein minor repeats and preventing malaria

L. T. Wang, N. K. Hurlburt, A. Schon, B. J. Flynn, L. S. Pereira, M. Dillon, Y. Flores-Garcia, B. Bonilla, F. Zavala, A. H. Idris, J. R. Francica, M. Pancera, R. A. Seder

This study shows that the L9 antibody's light chain is essential for binding PfCSP minor repeats and enhancing neutralization of malaria sporozoites.

bioRxiv · Aug 11, 2021Immunology

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