Author

J. E. Bowen

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· 14 Microbiology· 4 Biochemistry· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 21 Research Focus:host-pathogen & immune response· 18 Organism:human· 15 Assay:proteomics· 11 Research Focus:drug response / drug discovery· 5 Research Focus:cell type annotation· 4 Assay:structural biology· 4 Research Focus:protein structure prediction· 3

Frequent Co-Authors

A. C. Walls· 17 shared D. Veesler· 15 shared D. Corti· 12 shared M. A. Tortorici· 10 shared D. Pinto· 9 shared E. Cameroni· 9 shared G. Snell· 8 shared H. W. Virgin· 8 shared

Activity by Year

2020-2022 · peak 14/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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Curved chords = mutual co-authorship

17 shared papersImmunology

A. C. Walls

Mutual co-authors in cluster

Author profile →

21 papers

Recent·Most cited

Maturation of SARS-CoV-2 Spike-specific memory B cells drives resilience to viral escape

R. Marzi, J. Bassi, C. Silacci-Fregni, I. Bartha, F. Muoio, K. Culap, N. Sprugasci, G. Lombardo, C. Saliba, E. Cameroni, A. Cassotta, J. S. Low, A. C. Walls, M. McCallum, M. A. Tortorici, , L. Piccoli

The paper examines the kinetics, avidity, and cross-reactivity of SARS-CoV-2-specific memory B cells and antibodies in infected and vaccinated individuals over 16 months, finding that MBC maturation enhances resilience to viral escape.

bioRxiv · Sep 30, 2022Immunology

Imprinted antibody responses against SARS-CoV-2 Omicron sublineages

Y.-J. Park, D. Pinto, A. C. Walls, Z. Liu, A. De Marco, F. Benigni, F. Zatta, C. Silacci-Fregni, J. Bassi, K. R. Sprouse, A. Addetia, J. E. Bowen, C. Stewart, M. Giurdanella, C. Saliba, , Piccoli

This study shows that hybrid immunity and vaccine boosters provide potent neutralizing activity against Omicron BA.1 and BA.2, while breakthrough infections induce nasal mucosal neutralization and identify an ultrapotent pan-variant antibody.

bioRxiv · May 8, 2022Immunology

ACE2 engagement exposes the fusion peptide to pan-coronavirus neutralizing antibodies

J. S. Low, J. Jerak, M. A. Tortorici, M. McCallum, D. Pinto, A. Cassotta, M. Foglierini, F. Mele, R. Abdelnabi, B. Weynand, J. Noack, M. Montiel-Ruiz, S. Bianchi, F. Benigni, N. Sprugasci, , F. Sallusto

The paper identifies monoclonal antibodies that neutralize multiple coronaviruses by targeting the fusion peptide, which becomes exposed upon ACE2 engagement.

bioRxiv · Mar 30, 2022Immunology

Omicron BA.1 and BA.2 neutralizing activity elicited by a comprehensive panel of human vaccines

J. E. Bowen, K. R. Sprouse, A. C. Walls, I. G. Mazzitelli, J. K. Logue, N. M. Franko, K. Ahmed, A. Shariq, E. Cameroni, A. Gori, A. Bori, C. M. Posavad, J. M. Dan, Z. Zhang, D. Weiskopf, , D. Veesler

This study evaluates neutralizing activity against Omicron BA.1 and BA.2 variants elicited by various vaccines and finds that booster doses enhance neutralizing titers and breadth across all vaccine platforms.

bioRxiv · Mar 15, 2022 · PreprintImmunology

Structural changes in the SARS-CoV-2 spike E406W mutant escaping a clinical monoclonal antibody cocktail

A. Addetia, Y.-J. Park, T. Starr, A. J. Greaney, K. Sprouse, J. E. Bowen, S. W. Tiles, W. C. Van Voorhis, J. D. Bloom, D. Corti, A. C. Walls, D. Veesler

The paper examines structural changes in the SARS-CoV-2 spike E406W mutant that reduce neutralization by a monoclonal antibody cocktail and alters epitope recognition.

bioRxiv · Jan 21, 2022Biochemistry

Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement

M. McCallum, N. Czudnochowski, L. E. Rosen, S. K. Zepeda, J. E. Bowen, J. R. Dillen, A. Powell, T. Croll, J. Nix, H. W. Virgin, D. Corti, G. Snell, D. Veesler

This study determines the structural basis of SARS-CoV-2 Omicron's immune evasion and receptor engagement through cryo-EM and X-ray crystal structures of the spike and RBD bound to antibodies and ACE2.

bioRxiv · Dec 28, 2021Biochemistry

SARS-CoV-2 spike conformation determines plasma neutralizing activity

J. E. Bowen, A. C. Walls, A. Joshi, K. R. Sprouse, C. Stewart, M. A. Tortorici, N. M. Franko, J. K. Logue, I. G. Mazzitelli, S. W. Tiles, K. Ahmed, A. Shariq, G. Snell, N. T. Iqbal, J. Geffner, , D. Veesler

This study shows that vaccines encoding a prefusion-stabilized SARS-CoV-2 spike protein induce higher neutralizing antibody titers and better variant cross-neutralization compared to other vaccines or infection.

bioRxiv · Dec 19, 2021 · PreprintImmunology

Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift

E. Cameroni, C. Saliba, J. E. Bowen, L. E. Rosen, K. Culap, D. Pinto, L. A. VanBlargan, A. De Marco, S. K. Zepeda, J. di Iulio, F. Zatta, H. Kaiser, J. Noack, N. Farhat, N. Czudnochowski, , P

This study shows that Omicron variant's spike protein has enhanced ACE2 binding and reduces neutralizing activity, but some broadly neutralizing antibodies remain effective.

bioRxiv · Dec 12, 2021Immunology

Delta breakthrough infections elicit potent, broad and durable neutralizing antibody responses

A. C. Walls, K. R. Sprouse, A. Joshi, J. E. Bowen, N. Franko, M.-J. Navarro, C. Stewart, M. McCallum, E. A. Goecker, E. J. Degli-Angeli, J. Logue, A. Greninger, H. Chu, D. Veesler

The paper examines antibody responses in Delta breakthrough infections, finding they are more potent, durable, and broad compared to vaccinated-only or infected-only individuals.

bioRxiv · Dec 8, 2021 · PreprintImmunology

Antibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry

Y.-J. Park, A. De Marco, T. N. Starr, Z. Liu, D. Pinto, A. C. Walls, F. Zatta, S. K. Zepeda, J. E. Bowen, K. S. Sprouse, A. Joshi, M. Giurdanella, B. Guarino, J. Noack, R. Abdelnabi, , D. Veesler

This study identifies a broadly neutralizing antibody against sarbecoviruses that targets the ACE2 binding site and shows high resistance to escape mutations.

bioRxiv · Oct 13, 2021Immunology

A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy

A. J. Greaney, T. N. Starr, R. T. Eguia, A. N. Loes, K. Khan, F. Karim, S. Cele, J. E. Bowen, J. K. Logue, D. Corti, D. Veesler, H. Y. Chu, A. Sigal, J. D. Bloom

This study compares antibody responses to early SARS-CoV-2 isolates and the B.1.351 variant, finding shifts in immunodominance hierarchy within the spike receptor-binding domain.

bioRxiv · Oct 12, 2021Microbiology

Molecular basis of immune evasion by the delta and kappa SARS-CoV-2 variants

M. McCallum, A. C. Walls, K. R. Sprouse, J. E. Bowen, L. Rosen, H. V. Dang, A. deMarco, N. Franko, S. W. Tilles, J. Logue, M. C. Miranda, M. Ahlrichs, L. Carter, G. Snell, M. S. Pizzuto, , D. Veesler

This study investigates how delta and kappa SARS-CoV-2 variants evade immune responses by altering antigenic sites and reducing ACE2 binding affinity.

bioRxiv · Aug 11, 2021Immunology

A human antibody that broadly neutralizes betacoronaviruses protects against SARS-CoV-2 by blocking the fusion machinery

D. Pinto, M. M. Sauer, N. Czudnochowski, J. S. Low, M. A. Tortorici, M. P. Housley, J. Noack, A. C. Walls, J. E. Bowen, B. Guarino, L. E. Rosen, J. di Iulio, J. Jerak, H. Kaiser, S. Islam, , Lanzave

This paper identifies a human antibody that broadly neutralizes betacoronaviruses by targeting the stem helix, showing protection against SARS-CoV-2 and potential for vaccine design.

bioRxiv · May 9, 2021 · PreprintImmunology

Structural basis for broad sarbecovirus neutralization by a human monoclonal antibody

M. A. Tortorici, N. Czudnochowski, T. N. Starr, R. Marzi, A. C. Walls, F. Zatta, J. E. Bowen, S. Jaconi, J. di Iulio, Z. Wang, A. De Marco, S. Zepeda, D. Pinto, Z. Liu, M. Beltramello, , J. Bloom

This paper identifies a human monoclonal antibody that broadly neutralizes SARS-CoV-2 variants and zoonotic sarbecoviruses by targeting a conserved epitope on the spike protein.

bioRxiv · Apr 7, 2021 · PreprintImmunology

Antibodies to the SARS-CoV-2 receptor-binding domain that maximize breadth and resistance to viral escape

T. N. Starr, N. Czudnochowski, F. Zatta, Y.-J. Park, Z. Liu, A. Addetia, D. Pinto, M. Beltramello, P. Hernandez, A. J. Greaney, R. Marzi, W. G. Glass, I. Zhang, A. S. Dingens, J. E. Bowen, , Veesler

This study identifies antibodies against SARS-CoV-2 that balance neutralization potency and breadth, with some showing high resistance to viral escape.

bioRxiv · Apr 6, 2021 · PreprintMicrobiology

Membrane lectins enhance SARS-CoV-2 infection and influence the neutralizing activity of different classes of antibodies

F. A. Lempp, L. Soriaga, M. Montiel-Ruiz, F. Benigni, J. Noack, Y.-J. Park, S. Bianchi, A. C. Walls, J. E. Bowen, J. Zhou, H. Kaiser, M. Agostini, M. Meury, E. Dellota, S. Jaconi, , D. Corti

This study identifies membrane lectins that enhance SARS-CoV-2 infection and show how different antibodies neutralize infection through distinct mechanisms.

bioRxiv · Apr 3, 2021 · PreprintMicrobiology

SARS-CoV-2 immune evasion by variant B.1.427/B.1.429

M. McCallum, J. Bassi, A. De Marco, A. Chen, A. C. Walls, J. Di Iulio, M. A. Tortorici, M.-J. Navarro, C. Silacci-Fregni, C. Saliba, M. Agostini, D. Pinto, K. Culap, S. Bianchi, S. Jaconi, , D. Veesler

This study evaluates how the B.1.427/B.1.429 SARS-CoV-2 variant evades neutralizing antibodies through mutations in the RBD and NTD, showing reduced neutralization by both vaccine-induced and infection-derived antibodies.

bioRxiv · Mar 31, 2021 · PreprintImmunology

Elicitation of broadly protective sarbecovirus immunity by receptor-binding domain nanoparticle vaccines

A. C. Walls, M. C. Miranda, M. N. Pham, A. Schaefer, A. Greaney, P. S. Arunachalam, M.-J. Navarro, M. A. Tortorici, K. Rogers, M. A. O'Connor, L. Shireff, D. E. Ferrell, N. Brunette, E. Kepl, J. E. Bowen, , Veesler

This study shows that a SARS-CoV-2 RBD nanoparticle vaccine protects against SARS-CoV-2 and related sarbecoviruses, including variants, in mice and non-human primates.

bioRxiv · Mar 15, 2021Immunology

N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2

M. McCallum, A. De Marco, F. Lempp, M. A. Tortorici, D. Pinto, A. C. Walls, M. Beltramello, A. Chen, Z. Liu, F. Zatta, S. Zepeda, J. di Iulio, J. E. Bowen, M. Montiel-Ruiz, J. Zhou, , D. Veesler

The paper identifies a conserved antigenic supersite on the SARS-CoV-2 N-terminal domain recognized by neutralizing antibodies and shows its vulnerability to mutations in variants.

bioRxiv · Jan 14, 2021Immunology

Structural basis for broad coronavirus neutralization

M. Sauer, Y.-J. Park, M. A. Tortorici, A. C. Walls, L. Homad, O. Acton, J. E. Bowen, C. Wang, X. Xiong, W. de van der Schueren, J. Quispe, B.-J. Bosch, B. G. Hoffstrom, A. T. McGuire, D. Veesler

This study identifies a monoclonal antibody that broadly neutralizes multiple beta-coronaviruses by targeting a conserved epitope, providing a structural basis for designing pan-coronavirus vaccines.

bioRxiv · Dec 29, 2020Biochemistry

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