Biosketch

Dr. Alexander Belyy

Alexander studied biochemistry at the Lomonosov Moscow State University and obtained his Diploma in 2015. He then joined the group of Dr. Undine Mechold at the Institut Pasteur in Paris as a PhD student, where he worked on the ExoY effector from the human pathogen Pseudomonas aeruginosa. After his graduation in 2018, Alexander went to the Max-Planck Institute of Molecular Physiology in Dortmund for a postdoc in cryogenic electron microscopy (cryo-EM) with Prof. Stefan Raunser. There, his research was supported by the Humboldt Foundation and an EMBO postdoctoral fellowship and focused on the molecular mechanisms of bacterial toxins from Photorhabdus luminescens.

In August 2023, Alexander started a tenure-track assistant professor position at the Groningen Biomolecular Sciences & Biotechnology Institute (GBB). His research interest lies in the combination of microbiology, biochemistry and structural biology. By combining these disciplines, Alexander and his lab aims to reveal the structural basis of bacterial pathogenicity for development of novel therapeutic interventions.

Three top publications in 2020-2022:

1. Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin.

Belyy A, Lindemann F, Roderer D, Funk J, Bardiaux B, Protze J, Bieling P, Oschkinat H, Raunser S.

Nature Communications. 2022 Jul 20;13(1):4202. DOI: https://doi.org/10.1038/s41467-022-31836-w.

· The article was featured in a Nature Communications Editors’ Highlights webpage.

· Judged by online attention, the article is in the 97th percentile of all tracked articles of a similar age in all journals tracked by Altmetrics.

In this article, we show in atomic detail how Tc toxins modify the actin cytoskeleton by providing structural snapshots of the toxin’s activity.

2. Mechanism of actin-dependent activation of nucleotidyl cyclase toxins from bacterial human pathogens.

Belyy A, Merino F, Mechold U, Raunser S.

Nature Communications. 2021 Nov 16;12(1):6628. DOI: https://doi.org/ 10.1038/s41467-021-26889-2.

· According to Altmetrics, the article ranks in the top 5% of all studies in terms of the amount of attention it receives.

Human bacterial pathogens produce nucleotidyl cyclase toxins that become active only by binding to actin inside the target cells. In this article, we reported high-resolution cryo-EM structures of these toxins in complex with actin and revealed their activation mechanism in atomic detail.

3. Structure of the Lifeact-F-actin complex.

Belyy A, Merino F, Sitsel O, Raunser S.

PLoS Biology. 2020 Nov 20;18(11):e3000925. DOI: https://doi.org/10.1371/journal.pbio.3000925.

· The article is recommended by H1 connect and scores in the top 10% of articles in biological physics.

Lifeact is a popular probe for visualization the actin cytoskeleton. In this study, we determined the high-resolution cryo-EM structure of the Lifeact-F-actin complex and demonstrated that Lifeact directly competes with actin-binding proteins such as cofilin and myosin, providing an explanation for how Lifeact alters cell morphology. Thus, our results provide cell biologists with the background information to make an informed decision on whether to use Lifeact in an experiment. Our work laid the foundation for development of improved probes for live cell imaging.