Discovery to Understanding: Traditional and novel methods to understand the world of bacterial glycoproteins

TOPICAL COLLECTIONS

Guest Editors

Sue Twine

National Research Council Canada, Human Health Therapeutics Research , Director of Research & Development

Sue Twine is currently the Director of Research & Development at the National Research Council Canada’s Human Health Therapeutics Research Centre (NRC-HHT). Dr. Twine holds a BSc (Hons) and PhD in Biochemistry from the University of Southampton (Southampton, UK) and an MBA from Heriot-Watt University (Edinburgh, UK). Her research career began with the biochemical characterization of protein-ligand interactions. Upon joining the National Research Council, Dr. Twine refocussed her research toward the application of proteomics and mass spectrometry to improve her understanding of host-pathogen interactions. Most recently, Sue has led a diverse portfolio of projects, underpinned by the application of mass spectrometry technologies to improve the translation of disease understanding to tangible therapeutic applications. She has co-authored more than 50 research publications and served as a co-editor for several books too.

Kelly Fulton

National Research Council Canada, Human Health Therapeutics Research Centre

Kelly Fulton is a research scientist at the National Research Council Canada’s Human Health Therapeutics Research Centre (NRC-HHT). Kelly holds a BSc (Hons) degree in Biotechnology from the University of Ottawa (Ottawa, ON Canada) and is completing a PhD in Biochemistry at Carleton University (Ottawa, ON Canada). Her graduate research has focussed upon the development and application of methods to discover and characterize the bacterial glycoproteome. At NRC-HHT, she leads research projects in bacterial proteomics, supporting antimicrobial preparedness and vaccine development. Kelly has also led research into the application of mass spectrometry approaches for the improved characterization of complex protein- and viral-based therapeutics. In addition to research, Kelly has focussed on the development of early-career researchers, mentoring numerous undergraduate students. Kelly has authored over 30 publications and book chapters. She has also served as an editor for two books.

Collection Overview

The diversity of the proteome is significantly greater than the DNA of an organism suggests. This microheterogeneity is largely due to several post-transcriptional and post-translational modifications which allow for a greater combinatorial potential and subsequently greater functionality. One such modification that is present in all domains of life is glycosylation: the enzymatic addition of carbohydrate to the functional groups of amino acid side chains in proteins. This process may involve the addition of a single monosaccharide unit, or several monosaccharides linked together to form a glycan chain. Though glycoproteins are important for many biophysical properties and functions in both eukaryotic and prokaryotic organisms, the glycans modifying bacterial proteins typically include a more diverse range of carbohydrate moieties than those of eukaryotes. This makes studying bacterial glycoproteins more difficult, especially since most tools developed for glycoprotein analysis have historically been focused on eukaryotic systems.

In clinically relevant bacteria, glycoproteins are often virulence factors or otherwise associated with host-pathogen interactions and pathogenesis. Therefore, the discovery and characterization of bacterial glycoproteins hold significant clinical potential, with applications ranging from improved diagnostics to vaccine development.

Here, we present a Methods Collection of traditional and novel methods that may be used for the discovery of bacterial glycoproteins, as well as for the subsequent biophysical characterization and determination of biological significance. We hope this collection leads to an increased understanding of bacterial glycoproteins and their roles in pathogenesis.