Glycomics and Glycoproteomics

Clinical, pharmaceutical and biomedical research

Glycosylation plays important roles in immunity, development, infectious diseases and cancer. Analyzing and understanding the glycosylation changes associated with various pathological processes provides a way to the development of new therapeutic and diagnostic means. In the Glycomics and Glycoproteomics group, advanced analytical techniques are applied to study pathogen glycobiology as well as human glycobiology in health and disease.

Our group has a profound interest in Glycoimmunology, with a particular focus on antibody glycosylation. Human immunoglobulin G is the best studied group of glycoproteins with respect to its protein structure, but also regarding its posttranslational modifications, including glycosylation. We are intrigued by the vast influence of IgG glycosylation changes on the function of these biomolecules, and study the role and biomarker potential of antibody glycosylation in various disease settings.

Many developmental steps are known to involve glycosylation changes, and we aim at mapping the changes of the glycome in altered physiological states including developmental steps in early childhood, adolescence, and (healthy) aging. Also, we try to understand how the human glycome changes with metabolic switches and inflammatory processes.

Glycosylation in cancer is another key subject of our group. This research comprises the analysis of glycomic changes in tumor tissues, the characterization of glycosylated, circulating tumor antigens to evaluate their diagnostic potential, and the evaluation of the role of glycomic changes in promoting tumor progression and metastasis.

 

Analytical platforms and method development

Our group addresses a major bottleneck in glycobiological research, which is the lack of advanced glycomic analytical technology. To this end, we develop Targeted glycomics methods for studying e.g. antibody glycosylation. The major detection method is mass spectrometry, and we develop glycomic LC-MS and CE-MS workflows with a focus on miniaturization. Likewise, we explore MALDI-MS analysis of glycans and glycoconjugates relying on derivatization. Notably, our derivatization methods facilitate sialic acid isomer differentiation, thereby providing valuable insights in glycomic changes in inflammation and cancer. We recently moved into exploiting MALDI-MS analysis of glycans for analyzing the spatial distribution of glycans by glycan mass spectrometric imaging. Lastly, by automation of both sample preparation (robotization) and data processing, we are establishing workflows that can handle high numbers of clinical samples for glycomic analysis

Contact

Prof. Dr. Manfred Wuhrer
Phone: +31 (0)71 526 8744
Fax: +31 (0)71 526 6907
m.wuhrer@lumc.nl

Staff

Prof. Dr. Manfred Wuhrer
Dr. Yuri van der Burgt
Dr. Viktoria Dotz
Dr. David Falck
Noortje de Haan, MSc.
Ing. Agnes L. Hipgrave Ederveen
Christoph Gstöttner, MSc.
Guinevere Kammeijer, MSc.
Ing. Carolien A. M. Koeleman
Steffen Lippold, MSc.
Emanuela Lonardi, MSc.
Ana Momcilovic, MSc.
Alan Moran, BSc.
Lisa de Neef, BSc.
Dr. Simone Nicolardi
Ing. Jan Nouta
Tamas Pongrácz, MSc.
Thomas Sénard, MSc.
Dr. Elena Dominguez Vega
Gerda Vreeker, MSc.
Sander Wagt, MSc.
Wei Wang, MSc.
Dr. Tao Zhang