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Glycosylation is one of the most common and poorly understood forms of post-translational modification. Our aim is to understand the biochemical mechanisms underlying protein glycosylation, as well as decipher the roles that they play in health and disease.

Co-structures of DPAGT1 with its substrate allowed us to decipher is enzymatic mechanism

Protein glycosylation is essential to all eukaryotic life, and is present on most membrane and secreted proteins. However, we know little about the role of the vast majority of glycosylations. Irregularities in protein glycosylation can lead to a spectrum of diseases ranging from the devastating multisystem congenital diseases of glycosylation, to the milder congenital myasthenic syndromes, where patients suffer from abnormal neuromuscular junction development and function.

The aim of our group is to better understand the pathogenic mechanisms underlying these diseases of glycosylation, in order to find potential treatments. To do so, we use biochemical and cellular models to better understand how the dynamics of the glycosylation pathways change in disease, and how these changes affect the protein glycome. This will also allow us decipher the roles of protein glycosylations.

We work as part of a multidiscipline network using techniques in structural biology, biochemistry, molecular biology, cell biology, synthetic chemistry, and glycomics, to improve our understanding of glycosylation in health and disease.

Selected publications