Author

J. van Strijp

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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Microbiology· 7 Immunology· 1

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Research Focus:host-pathogen & immune response· 8 Approach:experimental assay· 7 Organism:human· 7 Assay:proteomics· 6 Organism:mouse· 2 Approach:benchmark study· 1 Research Focus:benchmarking· 1 Approach:biophysical modeling· 1

Frequent Co-Authors

C. J. C. de Haas· 5 shared K. P. M. van Kessel· 4 shared P. Aerts· 3 shared F. J. Beurskens· 2 shared J. Preiner· 2 shared J. Schuurman· 2 shared J. Strasser· 2 shared M. Ruyken· 2 shared

Activity by Year

2018-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 32 mutual co-author links

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5 shared papersMicrobiology

C. J. C. de Haas

Mutual co-authors in cluster

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8 papers

Recent·Most cited

LaeA-dependent production of small molecules of Aspergillus niger that compete with specific antibodies that bind to human immune receptors

N. Escobar, E. Keizer, J. van Neer, M. Arentshorst, J. van Strijp, P.-J. Haas, A. Ram, P. Punt, H. Wosten, H. de Cock

The paper identifies small molecules secreted by Aspergillus species that compete with antibodies binding to human immune receptors, with LaeA regulating some of these molecules.

bioRxiv · Apr 26, 2022 · PreprintMicrobiology

C1q binding to surface-bound IgG is stabilized by C1r2s2 proteases

S. A. Zwarthoff, K. Widmer, A. Kuipers, J. Strasser, M. Ruyken, P. Aerts, C. J. C. de Haas, D. Ugurlar, G. Vidarsson, J. van Strijp, P. Gros, P. Parren, K. P. M. van Kessel, J. Preiner, F. J. Beurskens, , S. H. M. Rooijakkers

This study shows that C1r2s2 proteases stabilize C1q binding to surface-bound IgG, with subclass-specific effects and improved phagocytosis with hexamer-enhanced IgGs.

bioRxiv · Feb 8, 2021Immunology

The impact of Staphylococcus aureus cell wall glycosylation on langerin recognition and Langerhans cell activation

A. Hendriks, R. van Dalen, S. Ali, D. Gerlach, G. A. van der Marel, F. F. Fuchsberger, P. Aerts, C. J. C. de Haas, A. Peschel, C. Rademacher, J. van Strijp, J. D. Codee, N. M. van Sorge

This study investigates how different glycosylation patterns on Staphylococcus aureus cell walls affect langerin recognition and Langerhans cell activation, finding that β-GlcNAc is sufficient for langerin binding regardless of its position on WTA.

bioRxiv · Nov 6, 2020Microbiology

Staphylococcal protein A inhibits complement activation by interfering with IgG hexamer formation

A. R. Cruz, M. A. den Boer, J. Strasser, F. J. Beurskens, C. J. C. de Haas, P. Aerts, G. Wang, R. N. de Jong, F. Bagnoli, J. van Strijp, K. P. M. van Kessel, J. Schuurman, J. Preiner, A. J. R. Heck, S. H. M. Rooijakkers

This study shows Staphylococcal protein A inhibits IgG hexamer formation, blocking complement activation, but IgG3 can still induce complement activation despite SpA.

bioRxiv · Jul 20, 2020Microbiology

Bacterial protein domains with a novel Ig-like fold bind human CEACAM receptors

N. M. van Sorge, D. A. Bonsor, L. Deng, E. Lindahl, V. Schmitt, M. Lyndin, A. Schmidt, O. R. Nilsson, J. Brizuela, E. Boero, E. J. Sundberg, J. van Strijp, K. S. Doran, B. S. Singer, G. Lindahl, A. J. McCarthy

This study identifies a novel Ig-like fold in bacterial adhesins that binds human CEACAM receptors, suggesting a broad mechanism for bacterial pathogenesis.

bioRxiv · Jun 9, 2020Microbiology

Bacterial immune evasion proteins: The therapeutic potential of CHIPS

A. Tromp, Y. Zhao, I. Jongerius, E. C. Heezius, P. Abrial, M. Ruyken, J. van Strijp, C. J. C. de Haas, A. Spaan, K. P. M. van Kessel, T. Henry, P.-J. A. Haas

This study evaluates CHIPS as a therapeutic agent for inflammation, showing promise in mice but safety concerns in humans due to pre-existing antibodies.

bioRxiv · Feb 25, 2020 · PreprintMicrobiology

Staphylococcus aureus toxin LukSF dissociates from its membrane receptor target to enable renewed ligand sequestration

K. Haapasalo, A. Wollman, C. de Haas, K. van Kessel, J. van Strijp, M. C. Leake

The paper shows Staphylococcus aureus toxin LukSF dissociates from its receptor to allow renewed ligand binding, facilitating rapid cell lysis and immune evasion.

bioRxiv · Apr 23, 2018Microbiology

Staphylococcal superantigen-like protein 13 activates neutrophils via Formyl Peptide Receptor 2

Y. Zhao, K. P. M. van Kessel, C. J. C. de Haas, M. R. C. Rogers, J. van Strijp, P.-J. Haas

This study shows SSL13 activates neutrophils through FPR2, acting as a chemoattractant and inducer of degranulation and oxidative burst, differing from other SSLs that inhibit immune responses.

bioRxiv · Apr 21, 2018Microbiology