Author

T. G. Caniels

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· 6 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Organism:human· 5 Research Focus:host-pathogen & immune response· 4 Assay:proteomics· 3 Research Focus:cell type annotation· 2 Research Focus:drug response / drug discovery· 2 Assay:flow cytometry· 1 Organism:non-human primate· 1

Frequent Co-Authors

R. W. Sanders· 6 shared M. J. van Gils· 5 shared A. B. Ward· 4 shared H. Liu· 4 shared I. A. Wilson· 4 shared J. L. Torres· 4 shared K. van der Straten· 4 shared M. Poniman· 4 shared

Activity by Year

2020-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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6 shared papersImmunology

R. W. Sanders

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Identification of new drugs to counteract anti-spike IgG-induced hyperinflammation in severe COVID-19

C. E. Geyer, H.-J. Chen, A. P. Bye, X. D. Manz, D. Guerra, T. G. Caniels, T. P. L. Bijl, G. R. Griffith, W. Hoepel, S. W. de Taeye, J. Veth, A. P. J. Vlaar, Amsterdam UMC COVID-19 Biobank, G. Vidarsson, H. J. Bogaard, , J. den Dunnen

The paper identifies SYK and PI3K inhibitors, particularly entospletinib, as effective in counteracting anti-spike IgG-induced hyperinflammation in severe COVID-19.

bioRxiv · Dec 20, 2022Immunology

Broad SARS-CoV-2 Neutralization by Monoclonal and Bispecific Antibodies Derived from a Gamma-infected Individual

D. Guerra, T. Beaumont, L. Radic, G. Kerster, K. van der Straten, M. Yuan, J. L. Torres, W.-H. Lee, H. Liu, M. Poniman, I. Bontjer, J. A. Burger, M. Claireaux, T. G. Caniels, J. L. Snitselaar, , M. J. van Gils

This study identifies broadly neutralizing monoclonal and bispecific antibodies from a Gamma variant-infected individual that effectively neutralize multiple SARS-CoV-2 variants.

bioRxiv · Oct 14, 2022Immunology

IgG1 responses following SARS-CoV-2 infection are polyclonal and highly personalized, whereby each donor and each clone displays a distinct pattern of cross-reactivity against SARS-CoV-2 variants

D. M. H. van Rijswijck, A. Bondt, M. Hoek, K. van der Straten, T. G. Caniels, M. Poniman, D. Eggink, C. B. E. M. Reusken, G. J. de Bree, R. W. Sanders, M. van Gils, A. J. R. Heck

The paper analyzes IgG1 clonal responses to SARS-CoV-2 variants in infected donors, finding unique and polyclonal antibody repertoires with varying cross-reactivity across variants.

bioRxiv · Feb 24, 2022Immunology

A public antibody class recognizes a novel S2 epitope exposed on open conformations of SARS-CoV-2 spike

M. Claireaux, T. G. Caniels, M. de Gast, J. Han, D. Guerra, G. Kerster, B. D. van Schaik, A. Jongejan, A. I. Schriek, M. Grobben, P. J. Brouwer, K. van der Straten, Y. Aldon, J. Capella-Pujol, J. L. Snitselaar, , M. J. van Gils

The paper identifies a novel S2 epitope recognized by a public antibody class in SARS-CoV-2-reactive B cells, which becomes exposed on vaccine-optimized spike proteins.

bioRxiv · Dec 1, 2021Immunology

Probing Affinity, Avidity, Anti-Cooperativity, and Competition in Antibody and Receptor Binding to the SARS-CoV-2 Spike by Single Particle Mass Analyses

V. C. Yin, S.-H. Lai, T. G. Caniels, P. J. M. Brouwer, M. Brinkkemper, Y. Aldon, H. Liu, M. Yuan, I. A. Wilson, R. W. Sanders, M. van Gils, A. J. R. Heck

This study uses single particle mass analyses to examine antibody binding to the SARS-CoV-2 spike protein, revealing sub-stoichiometric binding and its effectiveness in blocking ACE2.

bioRxiv · Jun 18, 2021Immunology

Two-component spike nanoparticle vaccine protects macaques from SARS-CoV-2 infection

P. J. M. Brouwer, M. Brinkkemper, P. Maisonnasse, N. Dereuddre-Bosquet, M. Grobben, M. Claireaux, M. de Gast, R. Marlin, V. Chesnais, S. Diry, J. D. Allen, Y. Watanabe, J. M. Griezen, G. Kerster, H. L. Turner, , de Bree

This paper develops a two-component spike nanoparticle vaccine that protects macaques from SARS-CoV-2 infection by inducing strong neutralizing antibodies and reducing viral replication.

bioRxiv · Nov 7, 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