Author

S. Bangaru

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· 7 Microbiology· 6 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 13 Research Focus:host-pathogen & immune response· 10 Assay:proteomics· 6 Organism:human· 5 Research Focus:cell type annotation· 3 Assay:structural biology· 3 Organism:virus· 3 Research Focus:drug response / drug discovery· 2

Frequent Co-Authors

A. B. Ward· 11 shared I. A. Wilson· 6 shared J. L. Torres· 6 shared M. Yuan· 5 shared N. C. Wu· 5 shared C.-C. D. Lee· 4 shared D. Huang· 4 shared D. Nemazee· 4 shared

Activity by Year

2018-2023 · peak 6/yr

Co-Author Collaboration Network

10 top collaborators · 44 mutual co-author links

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11 shared papersImmunology

A. B. Ward

Mutual co-authors in cluster

Author profile →

14 papers

Recent·Most cited

Deep repertoire mining uncovers ultra-broad coronavirus neutralizing antibodies targeting multiple epitopes

J. Hurtado, T. F. Rogers, D. B. Jaffe, B. Adams, S. Bangaru, E. Garcia, T. Capozzola, T. Messmer, P. Sharma, G. Song, N. Beutler, W. He, K. Dueker, R. Musharrafieh, M. J. T. Stubbington, , B. Briney

The paper identifies two broadly neutralizing antibodies against coronaviruses by screening B cell repertoires, showing they target different epitopes and offer protection against variants.

bioRxiv · Mar 28, 2023Immunology

Bispecific antibodies combine breadth, potency, and avidity of parental antibodies to neutralize sarbecoviruses

L. Radic, K. Sliepen, V. Yin, M. Brinkkemper, J. Capella-Pujol, A. I. Schriek, J. L. Torres, S. Bangaru, J. A. Burger, M. Poniman, I. Bontjer, J. H. Bouhuijs, D. Gideonse, D. Eggink, A. B. Ward, , J. Schinkel

This study shows bispecific antibodies combine the neutralizing breadth and potency of parental antibodies to neutralize SARS-CoV and SARS-CoV-2 variants, including Omicron.

bioRxiv · Nov 11, 2022Immunology

Structural mapping of antibody landscapes to human betacoronavirus spike proteins

S. Bangaru, A. Antanasijevic, N. Kose, L. M. Sewall, A. M. Jackson, N. Suryadevara, X. Zhan, J. L. Torres, J. Copps, A. Torrents de la Pena, J. E. Crowe, A. B. Ward

The paper maps epitopes of polyclonal antibodies against beta-coronavirus spike proteins in human sera, revealing cross-reactive patterns between seasonal and SARS-2 infections.

bioRxiv · Sep 30, 2021Immunology

Murine monoclonal antibodies against RBD of SARS-CoV-2 neutralize authentic wild type SARS-CoV-2 as well as B.1.1.7 and B.1.351 viruses and protect in vivo in a mouse model in a neutralization dependent manner

F. Amanat, S. Strohmeier, W.-H. Lee, S. Bangaru, A. B. Ward, L. Coughlan, F. Krammer

This study evaluates murine monoclonal antibodies against SARS-CoV-2 RBD, showing neutralization of wild-type and variants, and in vivo protection dependent on neutralization.

bioRxiv · Apr 5, 2021Microbiology

Ultrapotent bispecific antibodies neutralize emerging SARS-CoV-2 variants

H. Cho, K. K. Gonzales-Wartz, D. Huang, M. Yuan, M. Peterson, J. Liang, N. Beutler, J. L. Torres, Y. Cong, E. Postnikova, S. Bangaru, C. A. Talana, W. Shi, E. S. Yang, Y. Zhang, , J. Tan

This study identifies ultrapotent bispecific antibodies that neutralize emerging SARS-CoV-2 variants by targeting multiple spike protein regions, showing efficacy in vitro and in a hamster model.

bioRxiv · Apr 1, 2021 · PreprintImmunology

Structure and immune recognition of the porcine epidemic diarrhea virus spike protein

R. Kirchdoerfer, M. Bhandari, O. Martini, L. M. Sewell, S. Bangaru, K.-J. Yoon, A. Ward

The paper structures the PEDV spike protein using electron microscopy and characterizes the antibody response, revealing structural features and epitope dominance in the S1 region.

Structure · Apr 1, 2021Peer-reviewedBiophysics

A combination of cross-neutralizing antibodies synergizes to prevent SARS-CoV-2 and SARS-CoV pseudovirus infection

H. Liu, M. Yuan, D. Huang, S. Bangaru, C.-C. D. Lee, L. Peng, X. Zhu, D. Nemazee, M. J. van Gils, R. W. Sanders, H.-C. Kornau, S. M. Reincke, H. Pruss, J. Kreye, N. C. Wu, , I. A. Wilson

This study shows that combining cross-neutralizing antibodies CV38-142 and COVA1-16 enhances neutralization of SARS-CoV-2 and SARS-CoV pseudoviruses.

bioRxiv · Feb 11, 2021Microbiology

Canonical features of human antibodies recognizing the influenza hemagglutinin trimer interface

S. J. Zost, J. Dong, I. M. Gilchuk, P. Gilchuk, N. J. Thornburg, S. Bangaru, N. Kose, J. A. Finn, R. Bombardi, C. Soto, R. S. Nargi, R. P. Irving, N. Suryadevara, J. B. Westover, R. H. Carnahan, , J. E. Crowe

The paper identifies common genetic and structural features of human antibodies recognizing the influenza HA trimer interface, suggesting it as a target for vaccine design.

bioRxiv · Dec 31, 2020Immunology

A natural mutation between SARS-CoV-2 and SARS-CoV determines neutralization by a cross-reactive antibody

N. C. Wu, M. Yuan, S. Bangaru, D. Huang, X. Zhu, C.-C. D. Lee, H. L. Turner, L. Peng, L. Yang, D. Nemazee, A. B. Ward, I. A. Wilson

This study identifies a single amino acid mutation that determines the difference in neutralization ability of a cross-reactive antibody between SARS-CoV-2 and SARS-CoV.

bioRxiv · Sep 21, 2020Microbiology

Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate

S. Bangaru, G. Ozorowski, H. L. Turner, A. Antanasijevic, D. Huang, X. Wang, J. L. Torres, J. K. Diedrich, J.-H. Tian, A. D. Portnoff, N. Patel, M. J. Massare, J. R. Yates, D. Nemazee, J. C. Paulson, , A. B. Ward

The paper uses cryo-EM and glycan analysis to study the structure of a full-length SARS-CoV-2 spike protein in a vaccine candidate, revealing its stable prefusion conformation and novel trimer interactions.

bioRxiv · Aug 6, 2020Immunology

Cross-neutralization of a SARS-CoV-2 antibody to a functionally conserved site is mediated by avidity

H. Liu, N. C. Wu, M. Yuan, S. Bangaru, J. L. Torres, T. G. Caniels, J. van Schooten, X. Zhu, C.-C. D. Lee, P. J. M. Brouwer, M. J. van Gils, R. W. Sanders, A. B. Ward, I. A. Wilson

The paper identifies a SARS-CoV-2 antibody that cross-neutralizes SARS-CoV by binding a conserved epitope and relies on avidity for neutralization.

bioRxiv · Aug 2, 2020Microbiology

An alternative binding mode of IGHV3-53 antibodies to the SARS-CoV-2 receptor binding domain

N. C. Wu, M. Yuan, H. Liu, C.-C. D. Lee, X. Zhu, S. Bangaru, J. L. Torres, T. G. Caniels, P. J. M. Brouwer, M. J. van Gils, R. W. Sanders, A. B. Ward, I. A. Wilson

This study identifies an alternative binding mode of IGHV3-53 antibodies to the SARS-CoV-2 RBD, showing that longer CDR H3 can bind with different angles and interactions.

bioRxiv · Jul 26, 2020Microbiology

Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability

P. Brouwer, T. Caniels, K. van Straten, J. Snitselaar, Y. Aldon, S. Bangaru, J. Torres, N. Okba, M. Claireaux, G. Kerster, A. Bentlage, M. van Haaren, D. Guerra, J. Burger, E. Schermer, , M. van Gils

This study isolates potent neutralizing antibodies from COVID-19 patients that target multiple sites on the SARS-CoV-2 spike protein, offering insights for vaccine design and therapeutic development.

bioRxiv · May 12, 2020Microbiology

Potent anti-influenza H7 human monoclonal antibody induces separation of hemagglutinin receptor binding head domains

H. L. Turner, J. Pallesen, S. Lang, S. Bangaru, S. Urata, S. Li, C. A. Cottrell, C. A. Bowman, J. E. Crowe, I. A. Wilson, A. B. Ward

The paper identifies a transiently exposed epitope on influenza H7 hemagglutinin that is targeted by a potent neutralizing monoclonal antibody.

bioRxiv · Oct 5, 2018Immunology