We are interested in how unicellular eukaryote parasites exploit glycosylation to conduct their business, whether they accomplish this by modifying their own glycosylation, or employ glycan recognition to access their hosts. Our present attention is directed to the evolution and function of parasite glycosyltransferases, utilizing biochemistry in conjunction with gene editing and glycomic profiling to elucidate enzymatic and cellular roles. A major project is the role of cytoplasmic glycosylation in metabolic sensing of a range of aerobic unicellular model organisms and parasites.
- Msano Mandalasi, Hyun W. Kim, David Thieker, M. Osman Sheikh, Elisabet Gas-Pascual, Kazi Rahman, Peng Zhao, Nitin G. Daniel, Hanke van der Wel, H. Travis Ichikawa, John N. Glushka, Lance Wells, Robert J. Woods, Zachary A. Wood, and Christopher M. West. A terminal α3-galactose modification regulates an E3 ubiquitin ligase subunit in Toxoplasma gondii. J Biol Chem. 2020 May 15. pii: jbc.RA120.013792. doi: 10.1074/jbc.RA120.013792.