Author

J. Bimela

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 Biochemistry· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:host-pathogen & immune response· 5 Assay:structural biology· 4 Organism:human· 2 Research Focus:protein structure prediction· 2 Organism:virus· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

D. D. Ho· 6 shared G. Cerutti· 6 shared L. Shapiro· 6 shared P. D. Kwong· 6 shared J. Yu· 5 shared P. Wang· 5 shared E. R. Reddem· 4 shared L. Liu· 4 shared

Activity by Year

2020-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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6 shared papersImmunology

D. D. Ho

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

Structural Basis for Accommodation of Emerging B.1.351 and B.1.1.7 Variants by Two Potent SARS-CoV-2 Neutralizing Antibodies

G. Cerutti, M. Rapp, Y. Guo, F. Bahna, J. Bimela, E. R. Reddem, J. Yu, P. Wang, L. Liu, Y. Huang, D. D. Ho, P. D. Kwong, Z. Sheng, L. Shapiro

This study reports cryo-EM structures of two SARS-CoV-2 neutralizing antibodies bound to spike proteins of emerging variants, showing they retain potency despite RBD mutations.

bioRxiv · Feb 21, 2021Biochemistry

Modular basis for potent SARS-CoV-2 neutralization by a prevalent VH1-2-derived antibody class

M. Rapp, Y. Guo, E. R. Reddem, L. Liu, P. Wang, J. Yu, G. Cerutti, J. Bimela, F. Bahna, S. Mannepalli, B. Zhang, P. D. Kwong, D. D. Ho, L. Shapiro, Z. Sheng

The paper determines structures of three VH1-2-derived antibodies in complex with SARS-CoV-2 spike, revealing modular recognition mechanisms and conformational changes.

bioRxiv · Jan 11, 2021Immunology

Potent SARS-CoV-2 Neutralizing Antibodies Directed Against Spike N-Terminal Domain Target a Single Supersite

G. Cerutti, Y. Guo, T. Zhou, J. Gorman, M. Lee, M. Rapp, E. R. Reddem, J. Yu, F. Bahna, J. Bimela, Y. Huang, P. S. Katsamba, L. Lihong, M. S. Nair, R. Rawi, , L. Shapiro

This study identifies potent SARS-CoV-2 neutralizing antibodies targeting the N-terminal domain (NTD) and reveals they bind a common supersite on the spike protein.

bioRxiv · Jan 10, 2021Biochemistry

Paired heavy and light chain signatures contribute to potent SARS-CoV-2 neutralization in public antibody responses

B. B. Banach, G. Cerutti, A. S. Fahad, C.-H. Shen, M. Oliveira de Souza, P. S. Katsamba, Y. Tsybovsky, P. Wang, M. S. Nair, Y. Huang, I. M. Francino Urdaniz, P. J. Steiner, M. Gutierrez-Gonzalez, L. Liu, S. N. Lopez Acevedo, , B. J. DeKosky

This study identifies a public antibody class, IGHV3-53/3-66, with potent SARS-CoV-2 neutralization capabilities through paired heavy and light chain interactions.

bioRxiv · Dec 31, 2020Immunology

Potent Neutralizing Antibodies Directed to Multiple Epitopes on SARS-CoV-2 Spike

L. Liu, P. Wang, M. S. Nair, J. Yu, M. Rapp, Q. Wang, Y. Luo, J. F.-W. Chan, V. Sahi, A. Figueroa, X. V. Guo, G. Cerutti, J. Bimela, J. Gorman, T. Zhou, , D. D. Ho

The paper isolates and characterizes 61 SARS-CoV-2-neutralizing monoclonal antibodies from infected patients, identifying potent antibodies targeting multiple epitopes on the spike protein.

Nature · Jul 22, 2020Peer-reviewedMicrobiology

Cryo-EM Structures Delineate a pH-Dependent Switch that Mediates Endosomal Positioning of SARS-CoV-2 Spike Receptor-Binding Domains

T. Zhou, Y. Tsybovsky, A. S. Olia, J. Gorman, M. A. Rapp, G. Cerutti, G.-Y. Chuang, P. S. Katsamba, A. Nazzari, J. M. Sampson, A. Schon, P. D. Wang, J. Bimela, W. Shi, I.-T. Teng, , P. D. Kwong

This paper uses cryo-EM to show how SARS-CoV-2 spike protein undergoes pH-dependent structural changes that affect ACE2 binding and antibody evasion.

bioRxiv · Jul 4, 2020 · PreprintImmunology