A
Andrea N. Loes
Researcher at Fred Hutchinson Cancer Research Center
Publications - Â 28
Citations - Â 3564
Andrea N. Loes is an academic researcher from Fred Hutchinson Cancer Research Center. The author has contributed to research in topics: Epitope & Antibody. The author has an hindex of 11, co-authored 24 publications receiving 1638 citations. Previous affiliations of Andrea N. Loes include Arizona State University at the West campus & University of Oregon.
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Journal ArticleDOI
Comprehensive mapping of mutations in the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human plasma antibodies.
Allison J. Greaney,Allison J. Greaney,Andrea N. Loes,Andrea N. Loes,Katharine H.D. Crawford,Katharine H.D. Crawford,Tyler N. Starr,Tyler N. Starr,Keara D. Malone,Helen Y. Chu,Jesse D. Bloom,Jesse D. Bloom +11 more
TL;DR: In this article, the authors map how convalescent plasma antibodies are impacted by all mutations to the spike's receptor-binding domain (RBD), the main target of plasma neutralizing activity.
Journal ArticleDOI
Complete Mapping of Mutations to the SARS-CoV-2 Spike Receptor-Binding Domain that Escape Antibody Recognition.
Allison J. Greaney,Allison J. Greaney,Tyler N. Starr,Pavlo Gilchuk,Seth J. Zost,Elad Binshtein,Andrea N. Loes,Andrea N. Loes,Sarah K Hilton,John Huddleston,Rachel Eguia,Katharine H.D. Crawford,Katharine H.D. Crawford,Adam S. Dingens,Rachel S. Nargi,Rachel E. Sutton,Naveenchandra Suryadevara,Paul W. Rothlauf,Paul W. Rothlauf,Zhuoming Liu,Sean P. J. Whelan,Robert H. Carnahan,Robert H. Carnahan,James E. Crowe,James E. Crowe,Jesse D. Bloom,Jesse D. Bloom,Jesse D. Bloom +27 more
TL;DR: A deep mutational scanning method is described to map how all amino-acid mutations in the RBD affect antibody binding, and this method is applied to 10 human monoclonal antibodies to enable rational design of antibody therapeutics and assessment of the antigenic consequences of viral evolution.
Journal ArticleDOI
Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays.
Katharine H.D. Crawford,Katharine H.D. Crawford,Rachel Eguia,Adam S. Dingens,Andrea N. Loes,Keara D. Malone,Caitlin R Wolf,Helen Y. Chu,M. Alejandra Tortorici,M. Alejandra Tortorici,David Veesler,Michael L. M. Murphy,Deleah Pettie,Neil P. King,Alejandro B. Balazs,Jesse D. Bloom,Jesse D. Bloom,Jesse D. Bloom +17 more
TL;DR: It is demonstrated how these pseudotyped lentiviral particles could be used to measure the neutralizing activity of human sera or plasma against SARS-CoV-2 in convenient luciferase-based assays, thereby providing a valuable complement to ELISA-based methods that measure antibody binding rather than neutralization.
Posted ContentDOI
Protocol and reagents for pseudotyping lentiviral particles with SARS-CoV-2 Spike protein for neutralization assays
Katharine H.D. Crawford,Katharine H.D. Crawford,Rachel Eguia,Adam S. Dingens,Andrea N. Loes,Keara D. Malone,Caitlin R Wolf,Helen Y. Chu,M. Alejandra Tortorici,M. Alejandra Tortorici,David Veesler,Michael L. M. Murphy,Deleah Pettie,Neil P. King,Alejandro B. Balazs,Jesse D. Bloom,Jesse D. Bloom,Jesse D. Bloom +17 more
TL;DR: It is demonstrated how these pseudotyped lentiviral particles can be used to measure the neutralizing activity of human sera or plasma against SARS-CoV-2 in convenient luciferase-based assays, thereby providing a valuable complement to ELISA-based methods that measure antibody binding rather than neutralization.
Posted ContentDOI
Complete mapping of mutations to the SARS-CoV-2 spike receptor-binding domain that escape antibody recognition.
Allison J. Greaney,Allison J. Greaney,Tyler N. Starr,Pavlo Gilchuk,Seth J. Zost,Elad Binshtein,Andrea N. Loes,Andrea N. Loes,Sarah K Hilton,John Huddleston,Rachel Eguia,Katharine H.D. Crawford,Katharine H.D. Crawford,Adam S. Dingens,Rachel S. Nargi,Rachel E. Sutton,Naveenchandra Suryadevara,Paul W. Rothlauf,Paul W. Rothlauf,Zhuoming Liu,Sean P. J. Whelan,Robert H. Carnahan,James E. Crowe,Jesse D. Bloom,Jesse D. Bloom,Jesse D. Bloom +25 more
TL;DR: A deep mutational scanning method is described to map how all amino-acid mutations in the RBD affect antibody binding, and a complete escape-mutation maps enable rational design of antibody therapeutics and assessment of the antigenic consequences of viral evolution.