Author

M. Thepaut

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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Biochemistry· 3 Biophysics· 2 Immunology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Organism:E. coli· 3 Research Focus:protein folding & dynamics· 3 Assay:proteomics· 3 Research Focus:drug response / drug discovery· 2 Research Focus:host-pathogen & immune response· 2 Organism:bacteria (other)· 1 Research Focus:cell-cell communication· 1

Frequent Co-Authors

F. Fieschi· 6 shared A. Bernardi· 2 shared C. Vives· 2 shared D. Fenel· 2 shared G. Schoehn· 2 shared I. Bally· 2 shared N. Thielens· 2 shared A. Amen· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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6 shared papersBiochemistry

F. Fieschi

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

X-Ray Structure and enzymatic study of a Bacterial NADPHoxidase highlight the activation mechanism of eukaryoticNOX

I. Petit-Hartlein, A. Vermot, M. Thepaut, A.-S. Humm, F. Dupeux, J. Dupuy, V. Chaptal, J. A. Marquez, S. M. E. Smith, F. Fieschi

The paper presents crystal structures of SpNOX and its DH domain, revealing the activation mechanism of eukaryotic NOX by elucidating hydride transfer and flavin binding.

bioRxiv · Oct 16, 2023Biochemistry

The unique three-dimensional arrangement of Macrophage Galactose Lectin enables E. coli LipoPolySaccharides recognition through two distinct interfaces

M. Abbas, M. Maalej, F. Nieto Fabregat, M. Thepaut, J.-p. Kleman, I. Ayala, A. Molinaro, J.-P. Simorre, R. Marchetti, F. Fieschi, C. Laguri

The paper identifies two distinct glycan binding interfaces on Macrophage Galactose Lectin that enable high-affinity recognition of E. coli LipoPolySaccharides, independent of the canonical calcium-dependent site.

bioRxiv · Mar 2, 2023 · PreprintBiophysics

Rational control of structural off-state heterogeneity in a photoswitchable fluorescent protein provides switching contrast enhancement

V. Adam, K. Hadjidemetriou, N. Jensen, R. L. Shoeman, J. Woodhouse, A. Aquila, A.-S. Banneville, T. R. M. Barends, V. Bezchastnov, S. Boutet, M. Byrdin, M. Cammarata, S. Carbajo, N.-E. Christou, N. Coquelle, , Za

This paper enhances switching contrast in photoswitchable fluorescent proteins by modifying the V151 side chain, improving performance in RESOLFT nanoscopy.

ChemPhysChem · Aug 12, 2022Peer-reviewedBiophysics

Immunization with synthetic SARS-CoV-2 S glycoprotein virus-like particles protects Macaques from infection

G. Sulbaran, P. Maisonnasse, A. Amen, D. Guilligay, N. Bosquet, J. A. Burger, M. Poniman, M. Buisson, S. D. Dylon, T. Naninck, J. Lemaitre, W. Gros, A.-S. Gallouet, R. Marlin, C. Bouillier, , W. Weissenhorn

This study develops a synthetic SARS-CoV-2 S glycoprotein virus-like particle vaccine that protects macaques from infection through strong antibody and T cell responses.

bioRxiv · Jul 26, 2021Immunology

Safe and easy evaluation of tmRNA-SmpB-mediated trans-translation in ESKAPE pathogenic bacteria

M. Thepaut, R. Campos Da Silva, E. Renard, F. Barloy-Hubler, E. Ennifar, D. Boujard, R. Gillet

The paper develops a cell-free assay using GFP reassembly to evaluate trans-translation in ESKAPE bacteria for high-throughput screening and mechanistic studies.

bioRxiv · Dec 16, 2020Biochemistry

DC/L-SIGN recognition of spike glycoprotein promotes SARS-CoV-2 trans-infection and can be inhibited by a glycomimetic antagonist

M. Thepaut, J. Luczkowiak, C. Vives, N. Labiod, I. Bally, F. Lasala, Y. Grimoire, D. Fenel, S. Sattin, N. Thielens, G. Schoehn, A. Bernardi, R. Delgado, F. Fieschi

The paper shows DC/L-SIGN receptors on antigen-presenting cells enhance SARS-CoV-2 trans-infection, which can be blocked by a glycomimetic compound.

bioRxiv · Aug 9, 2020Immunology

Development Of C-Type Lectin Oriented Surfaces For High Avidity Glycoconjugates: Towards Mimicking Multivalent Interactions On The Cell Surface

V. Porkolab, C. Pifferi, I. Sutkeviciute, S. Ordanini, M. Taouai, M. Thepaut, C. Vives, M. Benazza, A. Bernardi, O. Renaudet, F. Fieschi

This paper develops SPR direct interaction assays for DC-SIGN to better assess multivalent glycocluster binding, showing that scaffold architecture, valency, and glycomimetic ligands are critical for achieving nanomolar affinities.

bioRxiv · Sep 24, 2019Biochemistry