The 2015 Eppendorf Edman Award: Benjamin Schulz

School of Chemistry and Molecular Biosciences
University of Queensland

Schulz After completing undergraduate degrees in Chemical Engineering and Biochemistry at the University of Queensland, I joined the Sydney-based biotechnology company Proteome Systems Ltd in 2001. In a team led by Professor Nicki Packer, I helped develop mass spectrometry-based proteomic and glycomic technologies, with a vision to making these powerful analytical approaches accessible to all researchers. I also used these technologies to investigate changes in protein glycosylation associated with cystic fibrosis lung disease. In 2004 I moved to Switzerland to undertake my doctoral studies at ETH Z├╝rich under the supervision of Professor Markus Aebi. Here, I used mass spectrometry glycoproteomics together with genetic approaches and in vitro biochemistry to study how protein glycosylation is regulated in bacteria, protozoa and yeast. I returned to Australia in 2008 for postdoctoral training in the laboratory of Professor Michael Jennings, supported by a University of Queensland Postdoctoral Research Fellowship and then an ARC Australian Postdoctoral Fellowship. My research during this time focused on unraveling the biosynthetic pathways of protein glycosylation in pathogenic bacteria and their role in immune evasion, especially in Neisseria meningitidis and Neisseria gonorrhoeae.

I started my own independent research group in the School of Chemistry and Molecular Biosciences at UQ as an NHMRC Career Development Fellow in 2012. The thriving bioscience research community at UQ provides an exceptional environment for my research, which also benefits from the wider opportunities offered by diverse national and international collaborations. Work in my group currently focuses on understanding the roles and regulation of protein glycosylation. As a complex posttranslational modification, the glycosylation status of proteins cannot be easily predicted from the genome. Instead, a central aspect of our research is to develop mass spectrometry-based techniques to identify and quantify the sugar structures and sites of modification on proteins from complex biological samples. As well as playing key fundamental roles in protein folding and function, changes in glycosylation can be useful biomarkers of disease in clinical settings. Research in my group therefore spans analytical method development, fundamental biology and biomarker discovery and translation. The Eppendorf Edman Award will allow me to attend the 2015 Gordon Research Conference on Posttranslational Modification Networks to be held in Hong Kong, China.