Marcelo Guerin
Marcelo Guerin
Ikerbasque Research Professor
Phone: 4337 / 944 061 309
Address: Bizkaia Science and Technology Park,
building 800, Derio (Bizkaia)

His interest in glycobiology began as an undergraduate student, while working with glycosyl hydrolases in the Leloir Institute at Buenos Aires, Argentina (1991-1996). This research center was named in honor to Luis F. Leloir, who discovered the first sugar nucleotide and was awarded the Nobel Prize in Chemistry in 1970 for his fundamental contributions to our knowledge of glycan biosynthesis and metabolism. He then completed his doctoral studies in biochemistry and molecular biology studying mechanistic aspects of glycosyltransferases in the Leloir Institute (1997-2002).

To further advance toward the understanding of the molecular mechanism that governs glycosyl transfer reactions, he moved to the Structural Biochemistry Unit at the Institut Pasteur in Paris, France, where he was first introduced to macromolecular crystallography (2003-2007). After this postdoctoral training, he continued his work on the mycobacterial cell envelope when he transferred as a postdoctoral fellow to the Mycobacteria Research Laboratories in the Department of Microbiology, at Colorado State University in the United States (2008-2009).

In 2009, he was awarded an Ikerbasque Research Professor position as the Head of the Structural Glycobiology Group (SGP). He started his work at the Unit of Biophysics, a joint center between the Spanish National Research Council (CSIC) and the University of the Basque Country, Spain. More recently, he moved to the Structural Biology Unit, CIC bioGUNE, at the Technological Park of Bizkaia, the Basque Country, Spain, as the Head of the Structural Glycobiology Lab. He is particularly interested in investigating the structural and mechanistic properties of carbohydrate modifying enzymes. To this end, the group is using a multidisciplinary approach including protein biochemistry, protein biophysics and structural biology.

The Structural Glycobiology Lab investigates the structural determinants and the modulation of substrate specificity of proteins involved in the biosynthesis and modification of glycans. They use a multidisciplinary approach including X-ray Crystallography, Small Angle X-ray Scattering, Electron Microscopy, Protein Biophysics, Protein Biochemistry and Molecular Biology, to elucidate mechanistic aspects of these processes at the molecular level. Research is concentrated - but not limited – on two main lines:

1. Carbohydrate-Modifying Enzymes

Most of the enzymes encoded in eukaryotic/prokaryotic/archaeans genomes that are responsible for the biosynthesis, degradation and modification of glycan structures are Carbohydrate-Modifying Enzymes, including: glycoside hydrolases (GHs), glycosyltransferases (GTs), polysaccharide lyases (PLs), carbohydrate esterases (CEs) and other auxiliary proteins (e.g. redox enzymes, carbohydrate binding modules). They are highly selective in nature, allowing the recognition of subtle structural differences in the sequences and stereochemistry of their carbohydrate substrates. In this context, the long-term goal of the Lab is to investigate the structural determinants and the modulation of substrate specificity of Carbohydrate-Modifying Enzymes at the molecular level.

2. The cell envelope of Mycobacterium tuberculosis

The cell envelope of M. tuberculosis contains glycans and lipids of exceptional structure that play prominent roles in the biology and pathogenesis of tuberculosis (TB). Consequently, the chemical structure and biosynthesis of the cell envelope is currently intensively studied in order to identify novel drug targets. The long-term goal of our Lab is (i) to investigate the mechanistic aspects of proteins involved in the biosynthesis of this particularly complex structure, and (ii) to understand in molecular detail the fundamental question of how the cell envelope is organized in space and time, within the context of its interaction with the host.