Glycobiology Advance Access published online on May 26, 2008
Glycobiology, doi:10.1093/glycob/cwn044
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Protein glycosylation pathways in filamentous fungi
1 Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, New South Wales, 2109, Australia
2 School of Biotechnology and Biomolecular Sciences, University of New South Wales, NSW 2052, Australia
3 Macquarie University Biotechnology Research Institute, Macquarie University, Sydney, New South Wales, 2109, Australia
* To whom correspondence should be addressed: Dr Nicolle Packer. Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, 2109, Australia. Tel: +61-2-9850-8176, +61-2-9850-8313; E-mail: nicki.packer{at}mq.edu.au
Received on December 20, 2007; accepted on May 17, 2008
Glycosylation of proteins is important for protein stability, secretion and localization. In this study, we have investigated the glycan synthesis pathways of 12 filamentous fungi including those of medical/agricultural/industrial importance for which genomes have been recently sequenced. We have adopted a systems biology approach to combine the results from comparative genomics techniques with high confidence information on the enzymes and fungal glycan structures, reported in the literature. From this, we have developed a composite representation of the glycan synthesis pathways in filamentous fungi (both N- and O-linked). The N-glycosylation pathway in the cytoplasm and endoplasmic reticulum was found to be highly conserved evolutionarily across all the filamentous fungi considered in the study. In the final stages of N-glycan synthesis in the Golgi, filamentous fungi follow the high mannose pathway as in Saccharomyces cerevisiae, but the level of glycan mannosylation is reduced. Highly specialized N-glycan structures with galactofuranose residues, phosphodiesters and other insufficiently trimmed structures have also been identified in the filamentous fungi. O-linked glycosylation in filamentous fungi was seen to be highly conserved with many mannosyltransferases that are similar to those in S. cerevisiae. However, highly variable and diverse O-linked glycans also exist. We have developed a web resource for presenting the compiled data with user friendly query options, which can be accessed at www.fungalglycans.org. This resource can assist attempts to remodel glycosylation of recombinant proteins expressed in filamentous fungal hosts.
Key words: Filamentous fungi / glycan synthesis / recombinant proteins / systems biology / comparative genomics
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