Trends in Glycoscience and Glycotechnology
Online ISSN : 1883-2113
Print ISSN : 0915-7352
ISSN-L : 0915-7352
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Volume 28, Issue 160
Displaying 1-6 of 6 articles from this issue
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MINIREVIEW
  • Classification and Comparison of Fucose-Binding Lectins Based on Their Structures
    Hisayoshi Makyio, Ryuichi Kato
    2016 Volume 28 Issue 160 Pages E25-E37
    Published: March 25, 2016
    Released on J-STAGE: March 25, 2016
    DOIhttps://doi.org/10.4052/tigg.1429.1E
    JOURNAL FREE ACCESS
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    Fucose-binding lectins play important roles in many biological processes including cell adhesion, infection of host cells by pathogenic bacteria, and binding to glycosylated proteins. Many three-dimensional structures of fucose-binding lectins have been reported. We compiled and compared the fucose-binding lectins whose structures have been solved to date. With the exception of three lone proteins, these lectins can be classified into six families. In this review, we describe the various fucose-binding mechanism of lectins based on their three-dimensional structures.
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  • Biosynthesis of Galactofuranose-containing Glycans in Filamentous Fungi
    Takuji Oka, Masatoshi Goto
    2016 Volume 28 Issue 160 Pages E39-E45
    Published: March 25, 2016
    Released on J-STAGE: March 25, 2016
    DOIhttps://doi.org/10.4052/tigg.1428.1E
    JOURNAL FREE ACCESS
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    Galactofuranose-containing glycans (Galf-glycans) are found in filamentous fungi, subphylum Pezizomycotina of Ascomycota. Although Galf-glycans have been broadly used as an indicator of pulmonary aspergillosis in clinical settings, and its importance in fungal cell growth is recognized, information pertaining to the galactofuranosyltransferase involved in the biosynthesis of Galf-glycans is sparse. In 2013, we identified and characterized the first galactofuranosyltransferase enzyme (GfsA) for the synthesis of Galf-glycans from a research model fungus, Aspergillus nidulans, and the human pathogen Aspergillus fumigatus. The enzyme belongs to the glycosyltransferase (GT) family 31. GfsA has the ability of transfer galactofuranose residues from the sugar donor UDP-galactofuranose to the non-reducing end of O-glycans in the Golgi apparatus. This review presents the process used to identify the enzyme, its enzymatic features, functions in the cell, and the biosynthesis of Galf-glycans in filamentous fungi.
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MEETING REPORT
MINIREVIEW (Jpn. Ed.)
  • Classification and Comparison of Fucose-Binding Lectins Based on Their Structures
    Hisayoshi Makyio, Ryuichi Kato
    2016 Volume 28 Issue 160 Pages J25-J38
    Published: March 25, 2016
    Released on J-STAGE: March 25, 2016
    DOIhttps://doi.org/10.4052/tigg.1429.1J
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    Fucose-binding lectins play important roles in many biological processes including cell adhesion, infection of host cells by pathogenic bacteria, and binding to glycosylated proteins. Many three-dimensional structures of fucose-binding lectins have been reported. We compiled and compared the fucose-binding lectins whose structures have been solved to date. With the exception of three lone proteins, these lectins can be classified into six families. In this review, we describe the various fucose-binding mechanism of lectins based on their three-dimensional structures.
    View full abstract
    Download PDF (5578K)
  • Biosynthesis of Galactofuranose-containing Glycans in Filamentous Fungi
    Takuji Oka, Masatoshi Goto
    2016 Volume 28 Issue 160 Pages J39-J45
    Published: March 25, 2016
    Released on J-STAGE: March 25, 2016
    DOIhttps://doi.org/10.4052/tigg.1428.1J
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    Galactofuranose-containing glycans (Galf-glycans) are found in filamentous fungi, subphylum Pezizomycotina of Ascomycota. Although Galf-glycans have been broadly used as an indicator of pulmonary aspergillosis in clinical settings, and its importance in fungal cell growth is recognized, information pertaining to the galactofuranosyltransferase involved in the biosynthesis of Galf-glycans is sparse. In 2013, we identified and characterized the first galactofuranosyltransferase enzyme (GfsA) for the synthesis of Galf-glycans from a research model fungus, Aspergillus nidulans, and the human pathogen Aspergillus fumigatus. The enzyme belongs to the glycosyltransferase (GT) family 31. GfsA has the ability of transfer galactofuranose residues from the sugar donor UDP-galactofuranose to the non-reducing end of O-glycans in the Golgi apparatus. This review presents the process used to identify the enzyme, its enzymatic features, functions in the cell, and the biosynthesis of Galf-glycans in filamentous fungi.
    View full abstract
    Download PDF (1474K)
MEETING REPORT (Jpn. Ed.)
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