Acquiring knowledge on the molecular structure and mode of action of a toxic protein is a critical step for the development of strategies aiming to fight or prevent its toxic effects.
Often a direct consequence of this knowledge is to allow taking advantage of the biological properties of a given toxin, turning the “bad guy” into a “good guy”, putting it to work as a therapeutic weapon, a diagnostic tool or a biochemical reagent.
Our interest in toxic proteins began with canatoxin, a neurotoxic protein we isolated in 1981 from jackbean Canavalia ensiformis seeds. After 20 years investigating the biological and molecular properties of canatoxin, we discovered that this protein is an isoform of UREASE.
Ureases are Multifunctional Toxins
Enzymes that catalyze the hydrolysis of urea to form one molecule of carbon dioxide and two molecules of ammonia are called urease (EC 126.96.36.199). Because of the release of ammonia, a highly reactive toxic compound, ureases are intrinsically toxic proteins.
Studying canatoxin we described, for the first time in 2001, toxic properties of ureases that are not related to their ability to release ammonia, thus characterizing these proteins as multifunctional toxins.
This virtual tour to our lab will guide you through the history of our encounter with ureases and the research topics we are working nowadays, organized in the topics as shown below:
In this virtual tour in LaNeurotox you will learn about how we first met ureases and the research lines we are currently working in our laboratories.
For references and access to full texts of our articles, please see selected publications or follow the link to Celia Carlini’s CV Lattes. External references are given at the end of each section.