Author

P. J. M. Brouwer

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· 4 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 12 Research Focus:host-pathogen & immune response· 11 Organism:human· 4 Assay:proteomics· 4 Assay:protein structure· 2 Assay:structural biology· 2 Organism:virus· 2 Approach:biophysical modeling· 1

Frequent Co-Authors

R. W. Sanders· 10 shared M. J. van Gils· 5 shared A. B. Ward· 4 shared J. A. Burger· 4 shared M. Crispin· 4 shared T. G. Caniels· 4 shared A. Antanasijevic· 3 shared H. Liu· 3 shared

Activity by Year

2020-2023 · peak 5/yr

Co-Author Collaboration Network

10 top collaborators · 32 mutual co-author links

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10 shared papersImmunology

R. W. Sanders

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Author profile →

12 papers

Recent·Most cited

Defining bottlenecks and opportunities for Lassa virus neutralization by structural profiling of vaccine-induced polyclonal antibody responses

P. J. M. Brouwer, H. R. Perrett, T. Beaumont, H. Nijhuis, S. Kruijer, J. A. Burger, W.-H. Lee, H. Muller-Krauter, R. W. Sanders, T. Strecker, M. J. van Gils, A. B. Ward

This study identifies neutralizing antibody epitopes against Lassa virus GPC using electron microscopy, revealing challenges in vaccine-induced responses and opportunities for improved vaccine design.

bioRxiv · Dec 21, 2023Immunology

Structural conservation of Lassa virus glycoproteins and recognition by neutralizing antibodies

H. R. Perrett, P. J. M. Brouwer, J. Hurtado, M. L. Newby, J. A. Burger, L. Liu, J. H. Bouhuijs, G. Gibson, T. Messmer, J. S. Schieffelin, A. Antanasijevic, G.-J. Boons, M. Crispin, R. W. Sanders, B. Briney, A. B. Ward

The paper structures and characterizes Lassa virus glycoproteins from multiple lineages and identifies neutralizing antibodies that target conserved epitopes.

bioRxiv · Sep 26, 2022Immunology

Lassa virus glycoprotein nanoparticles elicit a neutralizing antibody that defines a new site of vulnerability

P. J. M. Brouwer, A. Antanasijevic, A. J. Ronk, H. Mulller-Krauter, Y. Watanabe, M. Claireaux, N. M. Lloyd, T. P. L. Bijl, H. R. Perrett, T. H. Steijaert, J. A. Burger, M. M. van Haaren, K. Sliepen, M. van Gils, M. Crispin, , R. W. Sanders

This study develops Lassa virus glycoprotein nanoparticles that stabilize GPC trimers and elicit neutralizing antibodies targeting a new vulnerability site.

bioRxiv · Mar 28, 2022 · PreprintImmunology

SARS-CoV-2 infection activates dendritic cells via cytosolic receptors rather than extracellular TLRs

L. E. H. van der Donk, J. Eder, J. L. van Hamme, P. J. M. Brouwer, M. Brinkkemper, A. C. van Nuenen, M. J. van Gils, R. W. Sanders, N. A. Kootstra, M. Bermejo-Jambrina, T. B. H. Geijtenbeek

This study shows SARS-CoV-2 does not activate dendritic cells via extracellular TLRs but instead relies on intracellular sensors after infecting ACE2-expressing dendritic cells.

bioRxiv · Sep 2, 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

Antibody responses to SARS-CoV-2 mRNA vaccines are detectable in saliva

T. J. Ketas, D. Chaturbhuj, V. Cruz Portillo, E. Francomano, E. Golden, S. Chandrasekhar, G. Debnath, R. Diaz Tapia, A. Yasmeen, W. Leconet, Z. Zhao, P. J. M. Brouwer, M. M. Cushing, R. Sanders, A. Cupo, , J. P. Moore

This study detects S-protein and RBD-specific antibodies in saliva from mRNA-vaccinated healthcare workers after their second dose.

bioRxiv · Mar 11, 2021Microbiology

Site-specific steric control of SARS-CoV-2 spike glycosylation

J. D. Allen, H. Chawla, F. Samsudin, L. Zuzic, A. T. Shivgan, Y. Watanabe, W.-T. He, S. Callaghan, G. Song, P. Yong, P. J. M. Brouwer, Y. Song, Y. Cai, H. M. E. Duyvesteyn, T. Malinauskas, , M. Crispin

The paper compares glycosylation patterns of recombinant SARS-CoV-2 spike proteins across labs with infectious virus S protein, finding conserved site-specific glycan maturation stalling linked to protein structure.

bioRxiv · Mar 8, 2021 · PreprintBiochemistry

Immunofocusing and enhancing autologous Tier-2 HIV-1 neutralization by displaying Env trimers on two-component protein nanoparticles

P. J. M. Brouwer, A. Antanasijevic, M. de Gast, J. D. Allen, J. D. Allen, T. P. L. Bijl, A. Yasmeen, R. Ravichandran, J. Burger, G. Ozorowski, J. L. Torres, C. LaBranche, D. Montefiori, R. P. Ringe, M. van Gils, , R. W. Sanders

This study shows that displaying HIV-1 Env trimers on two-component protein nanoparticles enhances autologous Tier-2 neutralizing antibody titers in rabbits.

bioRxiv · Nov 30, 2020Microbiology

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

Afucosylated immunoglobulin G responses are a hallmark of enveloped virus infections and show an exacerbated phenotype in COVID-19

M. D. Larsen, E. L. de Graaf, M. E. Sonneveld, H. R. Plomp, F. Linty, R. Visser, M. Brinkhaus, T. Sustic, S. W. deTaeye, A. E. H. Bentlage, J. Nouta, S. Natunen, C. A. M. Koeleman, S. Sainio, N. A. Kootstra, , G. Vidarsson

The paper shows that afucosylated IgG responses are common in enveloped virus infections and are more severe in COVID-19, with implications for immune response and pathology.

bioRxiv · May 18, 2020Immunology