Subject
Our aim is to understand the multiple roles played by N-glycans in the proper folding and trafficking of secretory pathways proteins. We found that N-glycosylation is a main evolutionary driver that specifically shaped all secretory pathway proteins. In addition, we found how the chaperone and lectin systems that operate in the endoplasmic reticulum cooperate to assist along the complete folding pathway of glycoproteins. Currently, we are studying the molecular determinants that regulate de efficiency of N-glycan addition, which is modulated by both local and global factors. This knowledge will be useful to improve the industrial production of biopharmaceuticals. On the other hand, our lab studies the protein folding systems that operate in the parasite Trypanosoma cruzi, the agent that causes Chagas disease. In particular, we are studying the enzymes that catalyze the formation an isomerization of disulfide bridges, and their interaction with the N-glycan lectin systems. The global aim of this project is to find new targets for antichagasic drugs.

Approach
Our group uses a multidisciplinary approach to understand diverse aspects of protein biogenesis and folding in vivo. An important line of research focuses on protein N-glysosylation. This is one of the most abundant and drastic protein modifications, which affects nearly 25 % of the eukaryotic proteome.

Advances
Our lab is developing new molecular probes to study the biophysical conditions of cellular environments. In particular, we developed fluorescent sensor that quantify the macromolecular crowding level and are also useful to study basic aspects of liquid phase transitions in proteins.