Author

C. Planchais

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· 7 Biochemistry· 1

Signature Assays, Organisms & Methods

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Research Focus:host-pathogen & immune response· 15 Approach:experimental assay· 14 Organism:human· 9 Assay:proteomics· 9 Organism:virus· 3 Research Focus:cell type annotation· 2 Research Focus:benchmarking· 1 Assay:bulk RNA-seq· 1

Frequent Co-Authors

H. Mouquet· 14 shared O. Schwartz· 12 shared D. Planas· 10 shared T. Bruel· 10 shared F. Porrot· 9 shared F. Guivel-Benhassine· 8 shared I. Staropoli· 8 shared J. Buchrieser· 7 shared

Activity by Year

2020-2023 · peak 8/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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Curved chords = mutual co-authorship

14 shared papersMicrobiology

H. Mouquet

Mutual co-authors in cluster

Author profile →

15 papers

Recent·Most cited

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

Temperature sensitivity of bat antibodies links metabolic state with antigen-recognition diversity

N. Toshkova, V. Zhelyzkova, A. Reyes-Ruiz, E. Haerens, M. de Castro Deus, R. V. Lacombe, M. Lecerf, G. Gonzalez, N. Jouvenet, C. Planchais, J. D. Dimitrov

This study shows that bat antibodies change their antigen-binding properties with temperature, linking metabolic state to immune diversity and anti-inflammatory function.

bioRxiv · Aug 14, 2023Immunology

Resistance of Omicron subvariants BA.2.75.2, BA.4.6 and BQ.1.1 to neutralizing antibodies

D. Planas, T. Bruel, I. Staropoli, F. Guivel-Benhassine, F. Porrot, P. Maes, L. Grzelak, M. Prot, S. Mougari, C. Planchais, J. Puech, M. Saliba, R. Sahraoui, F. Femy, N. Morel, , O. Schwartz

This study evaluates the neutralizing antibody resistance of SARS-CoV-2 Omicron subvariants BA.2.75.2, BA.4.6, and BQ.1.1 to monoclonal antibodies and sera from vaccinated individuals.

bioRxiv · Nov 17, 2022Microbiology

Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2

C. Planchais, A. Reyes-Ruiz, R. Lacombe, A. Zarantonello, M. Lecerf, M. Revel, L. T. Roumenina, B. P. Atanasov, H. Mouquet, J. D. Dimitrov

The paper investigates how the SARS-CoV-2 spike protein's interaction with ACE2 evolved, revealing changes in binding dynamics and physicochemical forces across variants.

bioRxiv · Jun 11, 2022Biochemistry

IRF8 regulates efficacy of therapeutic anti-CD20 monoclonal antibodies

L. Grzelak, F. Roesch, A. Vaysse, A. Biton, F. Porrot, P.-H. Commere, C. Planchais, H. Mouquet, M. Vignuzzi, T. Bruel, O. Schwartz

This study identifies IRF8 as a regulator of CD20 expression and anti-CD20 antibody efficacy through CRISPR screening and functional validation in B cells.

bioRxiv · Jun 9, 2022Immunology

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

Structural insights of a highly potent pan-neutralizing SARS-CoV-2 human monoclonal antibody

J. L. Torres, G. Ozorowski, E. Andreano, H. Liu, J. Copps, G. Piccini, L. Donnici, M. Conti, C. Planchais, D. Planas, N. Manganaro, E. Pantano, I. Paciello, P. Pileri, T. Bruel, , A. B. Ward

The paper evaluates the potency of mAb J08 against SARS-CoV-2 variants using cell-based assays and cryo-EM, showing its resistance to escape mutations and broad binding capability.

Proceedings of the National Academy of Sciences · May 12, 2022Peer-reviewedImmunology

Potent Human Broadly SARS-CoV-2 Neutralizing IgA and IgG Antibodies Effective Against Omicron BA.1 and BA.2

C. Planchais, I. Fernandez, T. Bruel, G. Dias de Melo, M. Prot, M. Beretta, P. Guardado-Calvo, J. Dufloo, L. M. Molinos-Albert, M. Backovic, J. Chiaravalli, E. Giraud, B. Vesin, L. Conquet, L. Grzelak, , H. Mouquet

The paper identifies potent broadly neutralizing IgA and IgG antibodies against SARS-CoV-2 variants, including Omicron BA.1 and BA.2, from memory B cells in convalescents.

bioRxiv · Apr 1, 2022Immunology

An intranasal lentiviral booster broadens immune recognition of SARS-CoV-2 variants and reinforces the waning mRNA vaccine-induced immunity that it targets to lung mucosa

B. Vesin, J. Lopez, A. Noirat, P. Authie, I. Fert, F. Le Chevalier, F. Moncoq, K. Nemirov, C. Blanc, C. Planchais, H. Mouquet, F. Guinet, D. Hardy, C. Gerke, F. Anna, , P. Charneau

This study shows an intranasal lentiviral booster enhances and broadens immune response to SARS-CoV-2 variants and improves waning mRNA vaccine immunity in the lungs.

bioRxiv · Jan 30, 2022 · PreprintImmunology

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

Reduced sensitivity of infectious SARS-CoV-2 variant B.1.617.2 to monoclonal antibodies and sera from convalescent and vaccinated individuals

D. Planas, D. Veyer, A. Baidaliuk, I. Staropoli, F. Guivel-Benhassine, M. Rajah, C. Planchais, F. Porrot, N. Robillard, J. Puech, M. Prot, F. Gallais, P. Gantner, A. Velay, J. Le Guen, , O. Schwartz

This study shows that the SARS-CoV-2 B.1.617.2 variant is less sensitive to monoclonal antibodies and sera from convalescent and vaccinated individuals compared to other variants.

bioRxiv · May 26, 2021 · PreprintMicrobiology

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