ArticleBMC microbiology2012
High abundance of Serine/Threonine-rich regions predicted to be hyper-O-glycosylated in the secretory proteins coded by eight fungal genomes.
Article in BMC microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 41 citations in OpenAlex.
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- Comparative genomics reveals the presence of simple sequence repeats in genes related to virulence in plant pathogenic Pythium ultimum and Pythium vexans.Archives of microbiology · 2023Article
- Insights into the Structure of the Highly Glycosylated Ffase fromInternational journal of molecular sciences · 2022Article
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- CRZ1 transcription factor is involved in cell survival, stress tolerance, and virulence in fungi.Journal of biosciences · 2022Review
- Molecular basis of pathogenesis of postharvest pathogenic Fungi and control strategy in fruits: progress and prospect.Molecular horticulture · 2021Review
- SUN-Family ProteinFrontiers in microbiology · 2021Article
- Evolutionary analysis and protein family classification of chitin deacetylases in Cryptococcus neoformans.Journal of microbiology (Seoul, Korea) · 2020Article
- Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation.Nature communications · 2020Article
- Glycans as Modulators of Plant Defense Against Filamentous Pathogens.Frontiers in plant science · 2018Review
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- BcSUN1, aFrontiers in microbiology · 2017Article
- Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae.Molecular & cellular proteomics : MCP · 2016Article
- The Pmt2p-Mediated Protein O-Mannosylation Is Required for Morphogenesis, Adhesive Properties, Cell Wall Integrity and Full Virulence of Magnaporthe oryzae.Frontiers in microbiology · 2016Article
- Engineering yeast for producing human glycoproteins: where are we now?Future microbiology · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundO-glycosylation of secretory proteins has been found to be an important factor in fungal biology and virulence. It consists in the addition of short glycosidic chains to Ser or Thr residues in the protein backbone via O-glycosidic bonds. Secretory proteins in fungi frequently display Ser/Thr rich regions that could be sites of extensive O-glycosylation. We have analyzed in silico the complete sets of putatively secretory proteins coded by eight fungal genomes (Botrytis cinerea, Magnaporthe grisea, Sclerotinia sclerotiorum, Ustilago maydis, Aspergillus nidulans, Neurospora crassa, Trichoderma reesei, and Saccharomyces cerevisiae) in search of Ser/Thr-rich regions as well as regions predicted to be highly O-glycosylated by NetOGlyc (http://www.cbs.dtu.dk).
resultsBy comparison with experimental data, NetOGlyc was found to overestimate the number of O-glycosylation sites in fungi by a factor of 1.5, but to be quite reliable in the prediction of highly O-glycosylated regions. About half of secretory proteins have at least one Ser/Thr-rich region, with a Ser/Thr content of at least 40% over an average length of 40 amino acids. Most secretory proteins in filamentous fungi were predicted to be O-glycosylated, sometimes in dozens or even hundreds of sites. Residues predicted to be O-glycosylated have a tendency to be grouped together forming hyper-O-glycosylated regions of varying length.
conclusionsAbout one fourth of secretory fungal proteins were predicted to have at least one hyper-O-glycosylated region, which consists of 45 amino acids on average and displays at least one O-glycosylated Ser or Thr every four residues. These putative highly O-glycosylated regions can be found anywhere along the proteins but have a slight tendency to be at either one of the two ends.
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