Henning Paul-Julius Stahlberg

Positions: Since 2020 Prof. Physics, IPHYS, SB, EPFL, Switzerland 2009 – 2021 Prof. Structural Biology, Biozentrum, University Basel, Switzerland 2009 – 2010 Adj. Assoc. Prof. Molecular & Cellular Biology, UC Davis, CA, USA 2007 – 2009 Assoc. Prof. Molecular & Cellular Biology, UC Davis, CA, USA 2003 – 2007 Assist. Prof. Molecular & Cellular Biology, UC Davis, CA, USA Education: 2002 Habilitation, Biozentrum, University Basel, Switzerland 1997 – 2003 Postdoctoral Fellow, Biozentrum, University Basel, Switzerland 1992 – 1997 PhD Student, EPFL, Lausanne, Switzerland 1990 – 1991 Diploma Thesis in Solid State Physics, TU Berlin, Germany 1987 – 1993 Study of Physics, TU Berlin, Germany Selected Awards & Honors: 2009 W.M.Keck Award 2004 CAREER award, NSF, USA 2002 Habilitation, University Basel, Switzerland Selected Memberships: 2008 – 2013 Chancellor’s Fellow Award, UC Davis, CA, USA 2004 – 2009 Faculty of 1000 Since 1992 Swiss Society for Optics and Microscopy (SSOM)

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Microscopie électronique en transmission

vignette|upright=1.5|Principe de fonctionnement du microscope électronique en transmission. vignette|Un microscope électronique en transmission (1976). La microscopie électronique en transmission (ME

Cryomicroscopie électronique

vignette|Un microscope électronique en transmission (2003). La cryomicroscopie électronique (cryo-ME) correspond à une technique particulière de préparation d’échantillons biologiques utilisée en mic

Microscope électronique

thumb|Microscope électronique construit par Ernst Ruska en 1933.thumb|Collection de microscopes électroniques anciens (National Museum of Health & Medicine). Un microscope électronique (ME) est un ty

BIO-603(SH): Practical - Stahlberg Lab

Cryo-electron microscopy structural analysis of proteins. The course aims at demonstrating the workflow from sample purification to determining the atomic structure of a soluble or membrane protein.

PHYS-468: Physics of life

Life has emerged on our planet from physical principles such as molecular self-organization, thermodynamics, stochastics and iterative refinement. This course will introduce the physical methods to study life and will discuss the quantitative and physical concepts that make life possible.

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

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2.4-angstrom structure of the double-ring Gemmatimonas phototrophica photosystem

Henning Paul-Julius Stahlberg

Phototrophic Gemmatimonadetes evolved the ability to use solar energy following horizontal transfer of photosynthesis-related genes from an ancient phototrophic proteobacterium. The electron cryo-microscopy structure of the Gemmatimonas phototrophica photosystem at 2.4 angstrom reveals a unique, double-ring complex. Two unique membrane-extrinsic polypeptides, RC-S and RC-U, hold the central type 2 reaction center (RC) within an inner 16-subunit light-harvesting 1 (LH1) ring, which is encircled by an outer 24-subunit antenna ring (LHh) that adds light-gathering capacity. Femtosecond kinetics reveal the flow of energy within the RC-dLH complex, from the outer LHh ring to LH1 and then to the RC. This structural and functional study shows that G. phototrophica has independently evolved its own compact, robust, and highly effective architecture for harvesting and trapping solar energy.

AMER ASSOC ADVANCEMENT SCIENCE2022

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