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Personne

Priscilla Turelli

Biographie

Positions

2005-présent: Chercheur, Ecole Polytechnique Fédérale de Lausanne, Laboratoire de virologie et génétique, Suisse.

2001-2004: Chercheur dans le laboratoire du Pr D. Trono, Département de Microbiologie, Ecole de Médecine de Genève, Suisse.

1997-2001: Etudiante Post-doctorante dans le laboratoire du Pr D. Trono, Département de Microbiologie, Ecole de Médecine de Genève, Suisse.

Honneurs et prix

2004: Bristol-Myers Squibb AIDS AWARD

1997-1999: Human Frontier Science Program fellowship

Education

June 1997:

PhD in cellular biology.

Final mark:jury congratulations.

Université de la Méditerranée, France.

June 1993:

Post-graduate diploma in cellular biology and microbiology.

INSERM U372, Marseille-Luminy, université de Provence, France.

June 1992:

Master in cellular biology Specialty: genetic.

Final mark: Best master student of this year.

Université de la Méditerranée, France.

June 1987:

Scientific baccalaureate, France.

Enseignement

2009-présent: co-directeur de thèses, Ecole Polytechnique Fédérale de Lausanne, Suisse

2002: Tuteur en virologie pour les étudiants de médecine, Ecole de Médecine de Genève, Suisse.

1996-1997: Tuteur en biologie moléculaire et biochimie, Université de la Méditerranée, Aix Marseille II

Official source

https://people.epfl.ch/priscilla.turelli?lang=fr

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Domaines de recherche associés (37)

DNA methylation is a biological process by which methyl groups are added to the DNA molecule. Methylation can change the activity of a DNA segment without changing the sequence. When located in a g

The human genome is a complete set of nucleic acid sequences for humans, encoded as DNA within the 23 chromosome pairs in cell nuclei and in a small DNA molecule found within individual mitochondria.

thumb|Dessin représentant le doigt de zinc Cys2His2, consistant en une hélice alpha et un feuillet bêta aux brins antiparallèles. L'ion zinc est en vert, complexé à deux histidines (en bas) et deux cy

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Publications associées (47)

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Cryo-EM structures and binding of mouse and human ACE2 to SARS-CoV-2 variants of concern indicate that mutations enabling immune escape could expand host range

Kelvin Ka Ching Lau, Alexander Myasnikov, Sergey Nazarov, Dongchun Ni, Florence Pojer, Henning Paul-Julius Stahlberg, Didier Trono, Priscilla Turelli, Emiko Uchikawa

nvestigation of potential hosts of the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is crucial to understanding future risks of spillover and spillback. SARS-CoV-2 has been reported to be transmitted from humans to various animals after requiring relatively few mutations. There is significant interest in describing how the virus interacts with mice as they are well adapted to human environments, are used widely as infection models and can be infected. Structural and binding data of the mouse ACE2 receptor with the Spike protein of newly identified SARS-CoV-2 variants are needed to better understand the impact of immune system evading mutations present in variants of concern (VOC). Previous studies have developed mouse-adapted variants and identified residues critical for binding to heterologous ACE2 receptors. Here we report the cryo-EM structures of mouse ACE2 bound to trimeric Spike ectodomains of four different VOC: Beta, Omicron BA.1, Omicron BA.2.12.1 and Omicron BA.4/5. These variants represent the oldest to the newest variants known to bind the mouse ACE2 receptor. Our high-resolution structural data complemented with bio-layer interferometry (BLI) binding assays reveal a requirement for a combination of mutations in the Spike protein that enable binding to the mouse ACE2 receptor.

2023

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De novo design of protein interactions with learned surface fingerprints

Michael Bronstein, Stephen M Buckley, Bruno Emanuel Ferreira De Sousa Correia, Beat Fierz, Pablo Gainza Cirauqui, Sandrine Madeleine Suzanne Georgeon, Casper Alexander Goverde, Zander Harteveld, Anthony Marchand, Jane Marsden, Dongchun Ni, Elisa Oricchio, Aaron Simone Petruzzella, Charlène Mireille Raymonde Raclot, Stéphane Rosset, Andreas Scheck, Henning Paul-Julius Stahlberg, Freyr Sverrisson, Alexandra Teslenko, Didier Trono, Priscilla Turelli, Alexandra Krina Van Hall-Beauvais, Sarah Wehrle

Physical interactions between proteins are essential for most biological processes governing life. However, the molecular determinants of such interactions have been challenging to understand, even as genomic, proteomic and structural data increase. This knowledge gap has been a major obstacle for the comprehensive understanding of cellular protein–protein interaction networks and for the de novo design of protein binders that are crucial for synthetic biology and translational applications. Here we use a geometric deep-learning framework operating on protein surfaces that generates fingerprints to describe geometric and chemical features that are critical to drive protein–protein interactions10. We hypothesized that these fingerprints capture the key aspects of molecular recognition that represent a new paradigm in the computational design of novel protein interactions. As a proof of principle, we computationally designed several de novo protein binders to engage four protein targets: SARS-CoV-2 spike, PD-1, PD-L1 and CTLA-4. Several designs were experimentally optimized, whereas others were generated purely in silico, reaching nanomolar affinity with structural and mutational characterization showing highly accurate predictions. Overall, our surface-centric approach captures the physical and chemical determinants of molecular recognition, enabling an approach for the de novo design of protein interactions and, more broadly, of artificial proteins with function.

2023

Chargement

Anti-sars-cov-2 antibodies and use thereof in the treatment of sars-cov-2 infection

Didier Trono, Priscilla Turelli

The invention provides anti-SARS-CoV-2 antibodies and use thereof in prophylaxis, treatment and/or attenuation of a SARS-CoV-2 virus infection.

2022

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