Author

J. Buchrieser

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 10 Research Focus:host-pathogen & immune response· 10 Organism:human· 8 Assay:proteomics· 6 Research Focus:cell type annotation· 1 Organism:multiple species· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1

Frequent Co-Authors

O. Schwartz· 10 shared C. Planchais· 7 shared D. Planas· 7 shared H. Mouquet· 7 shared F. Porrot· 6 shared F. Guivel-Benhassine· 5 shared I. Staropoli· 5 shared N. Saunders· 5 shared

Activity by Year

2020-2024 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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10 shared papersMicrobiology

O. Schwartz

Mutual co-authors in cluster

Author profile →

10 papers

Recent·Most cited

Structural basis of TMPRSS2 zymogen activation and recognition by the HKU1 seasonal coronavirus

I. Fernandez, N. Saunders, S. Duquerroy, W. H. Bolland, A. Arbabian, E. Baquero, C. Blanc, P. Lafaye, A. Haouz, J. Buchrieser, O. Schwartz, F. A. Rey

This study determines the structure of HKU1-CoV receptor binding domain in complex with TMPRSS2, identifying key residues for host tropism and revealing the structural basis of TMPRSS2 activation.

bioRxiv · Feb 21, 2024Biochemistry

High fusion and cytopathy of SARS-CoV-2 variant B.1.640.1

W. Bolland, V. Michel, D. Planas, M. Hubert, F. Guivel-Benhassine, F. Porrot, I. Staropoli, M. N'Debi, C. Rodriguez, S. Fourati, M. Prot, C. Planchais, L. Hocqueloux, E. Simon-Loriere, H. Mouquet, , J. Buchrieser

This study characterizes the high fusogenicity and cytopathic effects of the SARS-CoV-2 B.1.640.1 variant, identifying mutations in the spike S2 domain responsible for these properties.

bioRxiv · Sep 6, 2023Microbiology

The spike-stabilizing D614G mutation interacts with S1/S2 cleavage site mutations to promote the infectious potential of SARS-CoV-2 variants

S. Gellenoncourt, N. Saunders, R. Robinot, L. Auguste, M. M. Rajah, J. Kervevan, R. Jeger-Madiot, I. Staropoli, C. Planchais, H. Mouquet, J. Buchrieser, O. Schwartz, L. A. Chakrabarti

This study shows the D614G mutation enhances the infectious potential of SARS-CoV-2 variants by synergizing with cleavage site mutations like P681H/R to increase spike fusogenicity.

bioRxiv · May 20, 2022Microbiology

Fusogenicity and neutralization sensitivity of the SARS-CoV-2 Delta sublineage AY.4.2

N. Saunders, D. Planas, W. H. Bolland, C. Rodriguez, S. Fourati, J. Buchrieser, C. Planchais, M. Prot, I. Staropoli, F. Guivel-Benhassine, F. Porrot, D. Veyer, H. Pere, N. Robillard, M. Saliba, , O. Schwartz

This study examines the fusogenicity and neutralization sensitivity of the SARS-CoV-2 AY.4.2 sublineage compared to the Delta variant, finding similar spike function but reduced neutralization sensitivity to certain antibodies and vaccines.

bioRxiv · Jan 7, 2022Microbiology

Considerable escape of SARS-CoV-2 variant Omicron to antibody neutralization

D. Planas, N. Saunders, P. Maes, F. G. Benhassine, C. Planchais, F. Porrot, I. Staropoli, F. Lemoine, H. Pere, D. Veyer, J. Puech, J. Rodary, W. H. Bolland, J. Buchrieser, G. Baele, , O. Schwartz

This study shows that the Omicron variant of SARS-CoV-2 is resistant to most monoclonal antibodies and vaccine-induced antibodies, with reduced neutralization compared to Delta.

bioRxiv · Dec 14, 2021Immunology

SARS-CoV-2 Alpha, Beta and Delta variants display enhanced Spike-mediated Syncytia Formation

M. M. Rajah, M. Hubert, E. Bishop, N. Saunders, R. Robinot, L. Grzelak, D. Planas, J. Dufloo, S. Gellenoncourt, A. Bongers, M. Zivaljic, C. Planchais, F. Guivel-Benhassine, F. Porrot, H. Mouquet, , O. Schwartz

This study compares syncytia formation by SARS-CoV-2 Alpha, Beta, and Delta variants to D614G, finding enhanced fusogenicity and differential effects of mutations on ACE2 binding and antibody escape.

bioRxiv · Jun 11, 2021Microbiology

Species-specific molecular barriers to SARS-CoV-2 replication in bat cells

S.-M. Aicher, F. Streicher, M. Chazal, D. Planas, D. Luo, J. Buchrieser, M. Nemcova, V. Seidlova, J. Zukal, J. Serra-Cobo, D. Pontier, O. Schwartz, J. Pikula, L. Dacheux, N. Jouvenet

The paper investigates SARS-CoV-2 replication in bat cells and finds species-specific molecular barriers, with some cells controlling viral replication after human ACE2 expression.

bioRxiv · May 31, 2021Microbiology

Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies

D. Planas, T. Bruel, L. Grzelak, F. Guivel-Benhassine, I. Staropoli, F. Porrot, C. Planchais, J. Buchrieser, M. M. Rajah, E. Bishop, M. Albert, F. Donati, S. Behillil, V. Enouf, M. Marianne, , O. Schwartz

This study assesses the neutralization sensitivity of SARS-CoV-2 B.1.1.7 and B.1.351 variants compared to D614G using sera and nasal swabs, finding reduced efficacy against B.1.351 in some convalescent and vaccinated individuals.

bioRxiv · Feb 12, 2021 · PreprintImmunology

Syncytia formation by SARS-CoV-2 infected cells

J. Buchrieser, J. Dufloo, M. Hubert, B. Monel, D. Planas, M. M. Rajah, C. Planchais, F. Porrot, F. Guivel-Benhassine, S. van der Werf, N. Casartelli, H. Mouquet, T. Bruel, O. Schwartz

This study shows SARS-CoV-2 infected cells form syncytia via Spike protein-mediated fusion, regulated by IFITMs and TMPRSS2.

The EMBO Journal · Nov 4, 2020Peer-reviewedMicrobiology

SUMOylation of SAMHD1 at Lysine 595 is required for HIV-1 restriction in non-cycling cells

C. Martinat, A. Cormier, J. Tobaly-Tapiero, N. Palmic, N. Casartelli, S. A. Coggins, J. Buchrieser, M. Persaud, F. Diaz-Griffero, L. Espert, G. Bossis, P. Lesage, O. Schwartz, B. Kim, F. Margottin, , A. Zamborlini

This study shows that SUMOylation of SAMHD1 at K595 is necessary for its antiviral activity in non-cycling cells, independent of its dNTPase function.

bioRxiv · Jun 4, 2020Microbiology