Immunoglobulin A (IgA) is an extensively glycosylated protein, which is increasingly gaining attention as a biopharmaceutical for the treatment of infectious diseases and cancer. However, only little is known about the role of glycosylation for the structure, as well as for the biophysical and immunological properties of IgA. With the tobacco related plant Nicotiana benthamiana it is possible to express recombinant glycoproteins with custom-made human-like N- and O-glycan modifications. This allows detailed investigation of structure-function relationships of different glycoforms.

IgA with distinct glycan modifications will be produced in N. benthamiana. The purified proteins will be analyzed by LC-ESI-MS to verify the glycan composition. The variants will then be investigated for their overall structure, conformational stability and thermal stability using size-exclusion chromatography combined with multi-angle light scattering (HPLC-MALS), circular dichroism (CD) spectroscopy and differential scanning calorimetry (DSC). Furthermore, the different glycoforms of IgA will be analyzed for receptor and antigen binding using surface-plasmon resonance spectroscopy.

Start: Soon as possible
Duration: 6-8 months
Salary: Minor employment (Geringfühgige Beschäftigung)
Supervisor: Assoc. Prof. Richard STRASSER,
Kathrin GÖRITZER

If you are interested please contact
Kathrin Göritzer (kathrin.goeritzer@boku.ac.at)