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1. (Article ID: 6623)
 
Neustroev KN, Golubev AM, Ibatullin FM, Moseichuk AV
Microheterogeneity in O-type sugar chains of carbohydrases secreted by Asp. awamori
Biochemistry and Molecular Biology International 30 (1993) 107-113
 

This paper deals with microheterogeneity in the structure of O-linked sugars of carbohydrases secreted by Asp. awamori, namely glucoamylase, α-galactosidase and α-glucosidase. Microheterogeneity was found to be related both to post-secretion deglycosylation and to changes in transferase activity induced by the differences in culturing conditions.

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2. (Article ID: 8117)
 
Deshpande N, Wilkins MR, Packer N, Nevalainen H
Protein glycosylation pathways in filamentous fungi
Glycobiology 18(8) (2008) 626–637
 

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.

synthesis, glycan, Recombinant Proteins, filamentous fungi, comparative genomics, systems biology

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