2007 Fiscal Year Final Research Report Summary
Molecular and structural biostudies on streptococcalinyasion/infection mechanisms to host cells through degradation of extracellular matrices glyoceaminoglycans
| Project/Area Number |
18580075
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Kyoto University |
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Principal Investigator |
HASHIMOTO Wataru Kyoto University, Grad. Schl.Agric, Associate Professor (30273519)
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| Project Period (FY) |
2006 – 2007
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| Keywords | Streptococcus / Glycosaminoalycan / Polysaccharide lyase / Unsaturated glucuronyl hydrolase / Invasion / infection mechanism / X-ray crystallography / Sulfated saccharide / Extracellular matrix |
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| Research Abstract |
Some pathogenic microorganisms produce polysaccharide-degrading enzymes (lyases and hydrolases) to invade mammalian and/or plant cells. Mammalian glycosaminoglycans that form part of cell surface matrix are typical targets for microbial enzymes. Unsaturated glucuronyl hydrolase (UGL), which was genetically first identified in Bacillus sp. strain GL1, catalyzes the hydrolytic release of an unsaturated uronic acid from oligosaccharides produced through the reaction of the matrix-degrading polysaccharide lyases (e.g., hyaluronate and chondroitin lyases), suggesting that these enzymes function as a virulent factor in microbial infection. In this study, structure and function relationship of glycosaminoglycan-degrading enzymes, lyase and hydrolase, was analyzed.
Based on X-ray crystallography of enzyme-substrate complexes and site-directed mutagenesis, mechanisms for catalytic reaction and substrate recognition of hyaluronate lyase homologue (xanthan lyase) were clarified. A single tyrosine
… More
residue abstracts C5-proton of the uronate residue at subsite +1 and donates the proton to glycosidic bond to be cleaved.
In contrast with general glycoside hydrolases with the retention or inversion catalytic mechanism of an anomeric configuration, UGL uniquely triggers hydrolysis of vinyl ether groups in the unsaturated uronate residue but not of the glycosidic bond.
Recent complete genome sequence analyses indicate that a large number of microorganisms ranging from bacteria to fungi (over 70 species) have a UGL homologous gene in their genome. In the Carbohydrate-Active enZyme (CAZy) database, UGL and its homologues form a new family, GH-88. Microbial producers of UGL include pathogenic bacteria such as clostridia, streptococci, and vibrios. The enzyme homologous gene has been found especially in streptococci, Streptococcus agalactiae, Streptococcus pneumoniae, Streptococcus pyogenes, and Streptococcus suis. Unlike the bacillus UGL, streptococcal UGL acts on unsaturated chondroitin disaccharide with a sulfate group at C4 of GalNAc. Less
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[Presentation] Structure and function of glycosaminoglycan-degrading enzyme from streptococci2007
Author(s)
Wataru, Hashimoto, Yukie, Maruyama, Takafumi, Itoh, Bunzo, Mikami, Kousaku, Murata
Organizer
Annual Meeting of Japan Society for Bioscience, Biotechnology, and Agrochemistry
Place of Presentation
Tokyo University of Agriculture
Year and Date
2007-03-26
Description
「研究成果報告書概要(欧文)」より
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[Presentation] Substrate recognition and catalytic mechanism of bacterial unsaturated galacturonyl hydrolase responsible for degradation of plant cell walls2007
Author(s)
Takafumi, Itoh, Akihito, Ochiai, Bunzo, Mikami, Wataru, Hashimoto, Kousaku, Murata
Organizer
Annual Meeting of Japan Society for Bioscience, Biotechnology, and Agrochemistry
Place of Presentation
Tokyo University of Agriculture
Year and Date
2007-03-26
Description
「研究成果報告書概要(欧文)」より
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[Presentation] A novel glycoside family 105 : Function and structure of Bacillus subtilis unsaturated galacturonyl hydrolase YteR responsible for plant cell wall degradation2006
Author(s)
Takafumi, Itoh, Akihito, Ochiai, Bunzo, Mikami, Wataru, Hashimoto, Kousaku, Murata
Organizer
Annual Meeting of Japan Society for Bioscience, Biotechnology, and Agrochemistry, Kansai Branch
Place of Presentation
Kyoto Institute of Technology
Year and Date
2006-10-01
Description
「研究成果報告書概要(欧文)」より
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[Presentation] Bacterial enzyme for degrading mammalian extracellular matrix : Function and structure of unsaturataed glucuronyl hydrolase2006
Author(s)
Takafumi, Itoh, Wataru, Hashimoto, Bunzo, Mikami, Kousaku, Murata
Organizer
Regular Meeting of Japan Society for Bioscience, Biotechnology, and Agrochemistry, Kansai Branch
Place of Presentation
Kyoto Prefectural University
Year and Date
2006-05-25
Description
「研究成果報告書概要(欧文)」より
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