MSACL 2019 US Abstract

Simultaneous Glycopeptide Profiling of Immunoglobulin G and A Reveals Glycan Changes in Colorectal Cancer

Ana Momčilović (1), Noortje de Haan(1), Lisa Anna de Neef(1), Agnes L. Hipgrave Ederveen(1), Rosina Plomp(1), Albert Bondt(1), Wilma E. Mesker (2), Viktoria Dotz(1), Manfred Wuhrer(1)
(1) Center for Proteomics and Metabolomics, Leiden University Medical Center, Postzone S3, Postbus 9600, 2300 RC Leiden, NL The Netherlands (2) Department of Surgery, Leiden University Medical Center, 2300 RC Leiden, The Netherlands

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Ana Momčilović (Presenter) Leiden University Medical Centre

Presenter Bio: I completed my Master degree in Molecular Biology and Physiology in Belgrade, Serbia with special interest on molecular biomedicine. Curiosity for glycobiology and strong motivation to broaden my skills in translational research led me to apply for a position in the Marie-Curie EU project “GlyCoCan”, where I am working as PhD student in the group of Prof. Dr. Manfred Wuhrer at the Center for Proteomics and Metabolomics at the Leiden University Medical Center in the Netherlands. During these last three years I was exposed to very different working environments, industry, clinic and academia. My research is focused on immunoglobulin G and immunoglobulin A glycosylation in colorectal cancer. Currently I am developing and applying high-throughput analytical techniques by using state-of-the-art instrumentation for the analysis of large biomolecules to answer clinically relevant questions.

Relevant Financial Disclosures (within past 24 months) No relevant financial relationship(s) to disclose. Discussing Products? NO, presenter will NOT present educational content related to products/services of the ineligible company(ies) listed above. Conflict mitigation NOT REQUIRED.

Immunoglobulin (Ig) A and G are serum glycoproteins playing important roles in the humoral immune defence. The functions of IgG and IgA are influenced by their glycosylation, a feature that is also associated with various pathologies. Here, we present a robust, high-throughput LC-MS platform for the simultaneous analysis of IgG and IgA glycopeptides, using minute amounts of serum. In a single LC-MS run, IgG Fc N-glycopeptides were separated and quantified in subclass-specific manner, together with seven glycopeptide clusters from IgA1 including the hinge region O-glycopeptide, IgA2, and joining chain. The method was applied on a cohort comprising 186 colorectal cancer cases and healthy controls each. A lower galactosylation in IgA1/2 Asn-144/Asn-131, IgA2 Asn-47 and IgG1, next to a lower IgA1 O-glycan sialylation was revealed in colorectal cancer patients as compared to healthy controls.