- Pauline M. Rudd - PI
- Barbara Keegan - PA/Administrator (to Professor Pauline M. Rudd)
Eoin Cosgrave, PhD – Fc Receptor Glycobiology
Principal Investigator
Post-Docs
- Giorgio Carta - Bioinformatics
- Eoin Cosgrave - Fc Receptor Glycobiology
- Margaret Doherty - Technology Development
- Eugene Dempsey - Cell signalling in Cancer
- Rebecca Duke - Glycobiology of O-linked glycans
- Mark Hilliard - Mass Spectrometry Development and Analytics
- Jayesh Kattla - Training and Research
- Karina Marino- Alimentary Glycoscience Research Cluster
- Niaobh O'Donoghue - Lab Manager
- John O'Rourke - Bioinformatics
- Oscar Potter - Technology Development
- Radka Saldova-Fahey - Glycobiology and Cancer
- Michael Schomberg - Technology Development
- Weston Struwe - Mass Spectrometry Development and Analytics
- Jayne Telford - Glycobiology and Disease
- Tharmala Tharmalingam - Reproductive Biology Research Cluster
Research Assistants
- Barbara Adamczyk - Glycobiology and Disease
- Patrick Jennings - Glycobiology and Disease
- Joanne Withers - Glycobiology and Disease
PhD Student
- Marie Galligan- Statistics
Former members
- Jonathan Bones
- Matthew Campbell
- Li Liu
- Jodie Abrahams
- Jennifer Byrne
- Marion Boland
- Ronan Kelly
- Ciara McManus
- Natalia Artemenko

Current Area of Interest
As a postdoctoral researcher with NIBRT, my project is directed towards the development of an Fc receptor (FcR) platform designed to assess the biological activity and efficacy of antibody-based therapeutics. It is now appreciated that the N-linked glycan located on Asn-297 of each Cγ2 domain of the two IgG heavy chains play an important role in co-ordinating immune effector functions such as antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC). These effector functions are mediated through interaction with specific receptors of the immune system, including the Fcγ receptor family (FcγRIa, FcγRIIa/b, and FcγRIIIa/b) and complement receptors MBL and C1q, which bind to the Fc region of IgG. The Fc-FcR interaction is a critical aspect of immunology as it links antigen recognition to antigen clearance. Our aim is to assess how changes in IgG glycosylation at Asn-297 influence its interaction with Fc receptors and what impact this has on the associated biological activity. The ability to engage specific Fc receptors has been of significant importance to the members of the biopharmaceutical industry intent on providing antibody-based therapies with a capacity of enhancing ADCC for the treatment of cancer.
Contact Information
Email:follow this link