Author
K. H. Crawford
Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
Biology Disciplines
Click to filter author papersSignature Assays, Organisms & Methods
Click to filter · or open tagActivity by Year
2020-2024 · peak 6/yrCo-Author Collaboration Network
10 top collaborators · 26 mutual co-author links10 papers
Recent·Most cited
Mapping the neutralizing specificity of human anti-HIV serum by deep mutational scanning
C. E. Radford, P. Schommers, L. Gieselmann, K. H. Crawford, B. Dadonaite, T. C. Yu, A. S. Dingens, J. Overbaugh, F. Klein, J. D. Bloom
This study maps the neutralizing specificity of human anti-HIV serum using deep mutational scanning to identify Env mutations affecting neutralization by polyclonal sera.
bioRxiv · Mar 23, 2023Immunology
A pseudovirus system enables deep mutational scanning of the full SARS-CoV-2 spike
B. Dadonaite, K. H. Crawford, C. E. Radford, A. G. Farrell, T. C. Yu, W. W. Hannon, P. Zhou, R. Andrabi, D. R. Burton, L. Liu, D. D. Ho, R. A. Neher, J. D. Bloom
This paper introduces a pseudovirus system for deep mutational scanning of SARS-CoV-2 spike protein mutations, showing how they affect antibody neutralization and infection.
bioRxiv · Oct 13, 2022Microbiology
The SARS-CoV-2 mRNA-1273 vaccine elicits more RBD-focused neutralization, but with broader antibody binding within the RBD
A. J. Greaney, A. N. Loes, L. E. Gentles, K. H. Crawford, T. N. Starr, K. D. Malone, H. Y. Chu, J. D. Bloom
The paper compares the specificity of antibodies from the mRNA-1273 vaccine and natural infection, finding vaccine antibodies are more RBD-focused but have broader epitope coverage within the RBD.
bioRxiv · Apr 14, 2021Microbiology
Comprehensive mapping of mutations to the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human serum antibodies
A. J. Greaney, A. N. Loes, K. H. Crawford, T. N. Starr, K. D. Malone, H. Y. Chu, J. D. Bloom
This study maps mutations in the SARS-CoV-2 RBD that affect recognition by polyclonal human serum antibodies, identifying key sites like E484 that significantly reduce neutralization.
bioRxiv · Dec 31, 2020Microbiology
Epitope profiling reveals binding signatures of SARS-CoV-2 immune response and cross-reactivity with endemic HCoVs
C. I. Stoddard, J. Galloway, H. Y. Chu, M. M. Shipley, H. L. Itell, C. R. Wolf, J. K. Logue, A. Magedson, K. Sung, M. Garrett, K. H. Crawford, U. Laserson, F. A. Matsen, Julie Overbaugh
This study maps SARS-CoV-2 antibody epitopes and identifies cross-reactive sequences with endemic HCoVs in COVID-19 patients.
bioRxiv · Oct 29, 2020 · PreprintImmunology
Complete mapping of mutations to the SARS-CoV-2 spike receptor-binding domain that escape antibody recognition
A. J. Greaney, T. N. Starr, P. Gilchuk, S. J. Zost, E. Binshtein, A. N. Loes, S. K. Hilton, J. Huddleston, R. Eguia, K. H. Crawford, A. S. Dingens, R. S. Nargi, R. E. Sutton, N. Suryadevara, P. W. Rothlauf, , J. D. Bloom
This study maps mutations in the SARS-CoV-2 spike RBD that escape antibody recognition, revealing escape mutation patterns and enabling the design of antibody cocktails.
bioRxiv · Sep 10, 2020Microbiology
Attenuated influenza virions expressing the SARS- CoV-2 receptor-binding domain induce neutralizing antibodies in mice
A. N. Loes, L. E. Gentles, A. J. Greaney, K. H. Crawford, J. D. Bloom
This paper describes an influenza-based vaccine for SARS-CoV-2 that induces neutralizing antibodies in mice comparable to natural infection.
bioRxiv · Aug 12, 2020Microbiology
Deep mutational scanning of SARS-CoV-2 receptor binding domain reveals constraints on folding and ACE2 binding
T. N. Starr, A. J. Greaney, S. K. Hilton, K. H. Crawford, M. J. Navarro, J. E. Bowen, M. A. Tortorici, A. C. Walls, D. Veesler, J. D. Bloom
The paper experimentally measures the effects of all amino-acid mutations in the SARS-CoV-2 RBD on protein folding and ACE2 binding, identifying constrained regions and tolerated mutations.
bioRxiv · Jun 17, 2020Microbiology
APOBEC3C tandem domain proteins create super restriction factors against HIV-1
M. M. McDonnell, K. H. Crawford, A. S. Dingens, J. D. Bloom, M. Emerman
The paper shows that synthetic tandem domain APOBEC3C proteins create more potent antiviral factors against HIV-1 than native A3C, with increased resistance to viral antagonism.
bioRxiv · Mar 27, 2020Microbiology