International Birnstiel Award 2023 celebrates six outstanding scientists
The fifth edition of the International Birnstiel Award for Doctoral Studies in Molecular Life Sciences has seen a flow of 103 excellent applications, many leading research organisations from around the world brought their top-talent forward. Six exceptionally talented and accomplished young scientists were selected to receive the award in the frame of a ceremony at the Vienna BioCenter next month: Sam van Beljouw (TU Delft), Ana Paredes (Spanish National Center for Cardiovascular Research - CNIC), Ariën Schiepers (The Rockefeller University), Ida Jentoft (Max Planck Institute for Multidisciplinary Sciences), Rosalie Lipsh-Sokolik (Weizmann Institute of Science), and Stanislau Yatskevich (MRC Laboratory of Molecular Biology / University of Cambridge).
103 institutions and PhD programmes from across the globe answered the call of the IMP and the Max Birnstiel Foundation to nominate their star PhD student of any molecular life science discipline from the previous year. In its fifth call, the accolade has become one of the most competitive awards of its kind. The Birnstiel Award is a treasure trove of brilliance, where the most promising stars of molecular life sciences shine.
“This call has attracted the most international set of nominations so far. We were happy to see a higher number of nominations from Asia and Australia than ever before. The Birnstiel Award has become internationally recognised and it shows,” said one member of the selection panel. “Choosing the awardees feels like trying to pick the best apple from a tree loaded with ripe contenders. We were flooded with fresh, exciting research that makes our job both thrilling and challenging!”
International Birnstiel Award: Laureates of 2023
The six awardees will receive a certificate, trophy, and prize of 2,000 Euro at a ceremony in Vienna later this year. While any academic institution in the world is entitled to submit a nomination, nominations are limited to one per institution or PhD programme. Due to this highly competitive selection process, the Birnstiel Award has become a highly prestigious recognition for emerging leaders in molecular life science research.
Sam van Beljouw, Technical University Delft
Supervisor: Stan Brouns
In his research on how the CRISPR-Cas system protects bacteria from invading viruses, Sam van Beljouw uncovered a remarkable protein complex named 'Craspase'. When Craspase detects specific viral RNAs, it transforms into a protein-cutter that causes a variety of possible outcomes, including the bacterium’s death. This seemingly peculiar bacterial suicide mode is, in fact, a clever strategy to prevent invading viruses from spreading to neighbouring cells. Craspase then also cuts the bound viral RNA, effectively deactivating its protein-cutting function. Thus, Craspase exhibits high precision in cleaving both RNA and protein, with the ability to self-regulate. Beyond its intriguing biological implications, Craspase is promising for applications demanding precise protein targeting, akin to the way Cas9 is employed for specific DNA targeting.
Sam van Beljouw studied biomedical engineering at TU Eindhoven and philosophy at Tilburg University. He then obtained a Master’s degree in molecular and cellular biotechnology from Wageningen University before starting his doctoral studies at TU Delft. His work was recognized by a Kiemprijs of the Dutch Royal Society for Microbiology (KNVM).
van Beljouw SPB, Haagsma AC, Rodríguez-Molina A, van den Berg DF, Vink JNA, Brouns SJJ. The gRAMP CRISPR-Cas effector is an RNA endonuclease complexed with a caspase-like peptidase. Science. 2021 Sep 17;373(6561):1349-1353. doi: 10.1126/science.abk2718.
Ana Paredes, Spanish National Center for Cardiovascular Research – CNIC
Supervisor: Mercedes Ricote
The mammalian heart requires a significant amount of energy to sustain cardiac beating. However, our understanding of how the heart's metabolism is regulated over time and space is limited. During her PhD, Ana Paredes made a crucial discovery – maternal milk plays a vital role in maturing the metabolism of murine newborn hearts. More specifically, an omega-6 fatty acid called γ-linolenic acid, found in maternal milk, triggers essential genetic programs that equip cardiac mitochondria with the required enzymes to consume lipids instead of glucose. This critical metabolic reprogramming enables the extrauterine heart beating and ultimately allows neonatal survival. Beyond cardiac health, these discoveries harbour significant implications for diseases where maternal-foetal harmony is disrupted.
Ana Paredes did her undergraduate studies in biochemistry at the University of Seville. She then obtained a Master’s degree in molecular biomedicine from the Autonomous University of Madrid, which also awarded her doctoral degree. Her research was supported by a CNIC fellowship and the Spanish Ministry of Education and Competitiveness.
Paredes A, Justo-Méndez R, Jiménez-Blasco D, Núñez V, Calero I, Villalba-Orero M, Alegre-Martí A, Fischer T, Gradillas A, Sant'Anna VAR, Were F, Huang Z, Hernansanz-Agustín P, Contreras C, Martínez F, Camafeita E, Vázquez J, Ruiz-Cabello J, Area-Gómez E, Sánchez-Cabo F, Treuter E, Bolaños JP, Estébanez-Perpiñá E, Rupérez FJ, Barbas C, Enríquez JA, Ricote M. γ-Linolenic acid in maternal milk drives cardiac metabolic maturation. Nature. 2023 Jun;618(7964):365-373. doi: 10.1038/s41586-023-06068-7.
Ariën Schiepers, The Rockefeller University
Supervisor: Gabriel D. Victora
Ariën Schiepers’ doctoral research focused on antibody responses against repeated exposure to viruses and their surface proteins. He and colleagues developed a series of novel techniques that represented breakthroughs in our ability to dissect antibody responses with unprecedented precision. He engineered mice to track the antibody-producing B cells as they undergo training to make better antibodies during the first response, tagging their memory descendants and the actual antibody molecules the descendants of this cohort of B cells will secrete. He found that, upon repeated boosting, the antibody response strongly favours reuse of the first cohort of B cells. New B cells, trained during the second response, only meaningfully contribute to subsequent antibody responses when induced by boosting with sufficiently divergent protein variants.
Ariën Schiepers studied biomedical sciences with a focus on infection and immunity at Utrecht University before joining The Rockefeller University. His doctoral research was supported by a fellowship of the Boehringer Ingelheim Fonds. His master thesis was awarded a best Master’s thesis prize by the Royal Holland Society of Sciences.
Schiepers A, van 't Wout MFL, Greaney AJ, Zang T, Muramatsu H, Lin PJC, Tam YK, Mesin L, Starr TN, Bieniasz PD, Pardi N, Bloom JD, Victora GD. Molecular fate-mapping of serum antibody responses to repeat immunization. Nature. 2023 Mar;615(7952):482-489. doi: 10.1038/s41586-023-05715-3.
Ida Jentoft, Max Planck Institute for Multidisciplinary Sciences
Supervisor: Melina Schuh
The very first stages of embryonic development are dependent on maternally inherited factors such as mRNA and proteins. Cytoplasmic lattices are long-lived filamentous structures specific to mammalian egg cells that are essential for early embryogenesis. In her PhD, Ida Jentoft investigated whether cytoplasmic lattices are important for storing maternal proteins to ensure their faithful inheritance to the embryo. To do this, she compared the proteome of mouse eggs with and without cytoplasmic lattices. She found that several proteins needed in the early embryo are depleted when cytoplasmic lattices are missing. In normal eggs, these proteins are enriched on the cytoplasmic lattice filaments. This suggests that the cytoplasmic lattices serve as a mammalian maternal protein storage compartment.
Before joining the Max Planck Institute for Multidisciplinary Sciences, Ida Jentoft studied molecular biomedicine at the University of Copenhagen – and one year of French literature at the Université Paul-Valéry Montpellier. For her doctoral studies, she was awarded a fellowship from the Boehringer Ingelheim Fonds.
Ida M. A. Jentoft, Felix J. B. Bäuerlein, Luisa M. Welp, Benjamin H. Cooper, Arsen Petrovic, Chun So, Sarah Penir, Yehor Horokhovskyi, Iina Takala,Heike Eckel, Rüdiger Moltrecht, Tommaso Cavazza, Juliane Liepe, Nils Brose, Henning Urlaub, Rubén Fernández‐Busnadiego, Melina Schuh: Oocytes enrich and store essential embryonic proteins on cytoplasmic lattices. Accepted for publication.
Rosalie Lipsh-Sokolik, Weizmann Institute
Supervisor: Sarel Fleishman
Enzymes are complex proteins that catalyse important biochemical reactions. In her PhD, Rosalie Lipsh-Sokolik studied the structural features that determine the mutational tolerance of enzymes. She then developed a new approach that uses structure-based simulations, phylogenetic analysis, and machine learning to dramatically change enzyme activity. For instance, her design approach generated highly efficient enzymes that break down venomous nerve agents and other synthetic pollutants. Furthermore, she developed new methods for designing huge repertoires of enzymes, isolating more than 10,000 functional ones in a single experiment. This work has the potential to enable the development of new enzymes with a wide range of applications in medicine, agriculture, and environmental remediation.
Rosalie Lipsh-Sokolik graduated from Jerusalem College of Technology in bioinformatics before joining the Weizmann Institute. Her doctoral research was supported by an Ariane de Rotschild scholarship. She was also recognised by a President’s Excellence Award of the Lev Academic Center.
Lipsh-Sokolik R, Khersonsky O, Schröder SP, de Boer C, Hoch SY, Davies GJ, Overkleeft HS, Fleishman SJ. Combinatorial assembly and design of enzymes. Science. 2023 Jan 13;379(6628):195-201. doi: 10.1126/science.ade9434.
Stanislau Yatskevich, MRC Laboratory of Molecular Biology / University of Cambridge
Supervisor: David Barford
Our cells use large and intricate macromolecular machines to accurately pass genetic information to two daughter cells during cell division. Errors during chromosome segregation often result in genetic abnormalities. Stanislau Yatskevich’s work focused on kinetochores, giant complexes that mediate attachment of mitotic spindle to chromosomes, and he showed that inner kinetochore forms a nucleosome-like particle that completely entraps the linker DNA of centromeric chromatin. Topological entrapment of the DNA by the inner kinetochore immediately addressed a long-standing question of how kinetochores withstand both pushing and pulling forces exerted by the mitotic spindle. Together with atomic structures of the outer kinetochore, his work addressed almost all details of the complete human kinetochore assembly.
Stanislau Yatskevich graduated in biochemistry from the University of Oxford before taking up his PhD studies at the MRC Laboratory of Molecular Biology as a student of the University of Cambridge. He, too, was supported by a Boehringer Ingelheim Fonds fellowship and was also awarded the Max Perutz Prize of the LMB.
Yatskevich S, Muir KW, Bellini D, Zhang Z, Yang J, Tischer T, Predin M, Dendooven T, McLaughlin SH, Barford D. Structure of the human inner kinetochore bound to a centromeric CENP-A nucleosome. Science. 2022 May 20;376(6595):844-852. doi: 10.1126/science.abn3810.
Due to the high number of outstanding nominations, many strong candidates could not be acknowledged with an award. The selection committee highlighted an additional seven scientists from the shortlist as "honourable mentions" to give them special recognition:
Alejandro Aguilera Castrejon, Weizmann Institute of Science
Supervisor: Jacob Hanna
Agneesh Barua, Okinawa Institute of Science and Technology (OIST)
Supervisor: Vincent Laudet
Larissa Dietz, University of Oxford
Supervisor: Paul R. Elliott
Agata Izabela Kalita, Institute of Molecular Biology
Supervisor: Claudia Isabelle Keller Valsecchi
Daniel Michelson, Harvard University
Supervisor: Diane Mathis
Mark Pownall, Yale University
Supervisor: Antonio Giraldez
Bhargav Sanketi, Cornell University
Supervisor: Natasza Kurpios
About Max Birnstiel and the Birnstiel Foundation
Max Luciano Birnstiel (1933 – 2014) was a molecular biologist and founding director of the Research Institute of Molecular Pathology (IMP). In this role, he made a major contribution to the exceptional academic standing of the IMP. He retired from his post as director in 1996.
Birnstiel’s research focused on gene regulation in eukaryotes. His lab was the first to purify single genes, the ribosomal RNA genes from the frog Xenopus laevis, in the late 1960s. Birnstiel was one of the first scientists to study how gene expression is regulated. He is also recognised for one of the earliest discoveries of a gene enhancer element, which his lab published in 1980. As a science manager, Birnstiel was a visionary who not only set the IMP on track to achieving research excellence, but he was also a vital force behind raising the profile of the Vienna BioCenter, now one of Europe’s most dynamic life science hubs with more than 2,650 people from 80 countries, working in 141 research groups and over 30 biotech companies.
Throughout his life, Max Birnstiel was a supporter of young talent and fostered an egalitarian culture at the IMP. It was in this spirit that a foundation bearing his name was set up in 2018. The Max Birnstiel Foundation co-funds initiatives and activities that support young scientists in molecular life sciences, such as the Vienna BioCenter Summer School and the International Birnstiel Award for Doctoral Studies in Molecular Life Sciences. www.maxbirnstiel.org, www.imp.ac.at/birnstiel-award