Maria Veiga da Cunha
is both a senior FRS-FNRS researcher at the de Duve Institute and an assistant professor at the School of Biomedical Sciences, UCLouvain, in Brussels, Belgium. She holds a degree in bioengineering from UCLouvain and a PhD from the University of Oxford. For the past 30 years, her research has focused on various inborn errors of metabolism together with her mentor Prof. Emile Van Schaftingen. Together, they explored various aspects of intermediary metabolism, focusing on the molecular identification and regulatory mechanisms of multiple enzymes. A key achievement of their work was pioneering research on metabolite repair, beginning with the identification of L-2-hydroxyglutarate deficiency as the first inborn error in this field. Importantly, she has made two major contributions to the field of GSD1b: (1) the discovery of the gene encoding the glucose-6-phosphate transporter of the endoplasmic reticulum (SLC37A4), which is mutated in GSD1b patients. This discovery enabled genetic screening for GSD1b. (2) The elucidation of the mechanism underlying neutropenia in GSD1b and G6PC3 deficiency, which led to the repurposing of the commonly used antidiabetic drug empagliflozin to treat neutropenia, first in a mouse model and subsequently in patients.
Together with Dr. Saskia Wortmann and other collaborators, she played a key role in initiating the use of empagliflozin to treat neutropenia in GSD1b patients. This work also led her to identify SGLT5, the renal transporter responsible for the reabsorption of 1,5-anhydroglucitol, a polyol whose presence in blood is responsible for these patient’s neutropenia. Since then, she has continued to focus part of her research on better understanding the toxicity of 1,5-anhydroglucitol on the neutrophils of GSD1b patients, with the goal of further improving available treatments.
She is also a specialist in hexokinase regulation and is actively investigating the mechanisms underlying two newly identified neurometabolic disorders with brain anomalies: PGM2L1 deficiency and NEDVIBA, caused by de novo mutations in hexokinase 1.
Affiliations