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  • Towards understanding the functional role of the glycosyltransferases involved in the biosynthesis of Moraxella catarrhalis lipooligosaccharide

    Author(s)
    Peak, Ian R
    Grice, ID
    Faglin, Isabelle
    Klipic, Zoran
    Collins, Patrick M
    van Schendel, Lucien
    Hitchen, Paul G
    Morris, Howard R
    Dell, Anne
    Wilson, Jennifer C
    Griffith University Author(s)
    Grice, Darren D.
    Wilson, Jenny C.
    Peak, Ian
    Year published
    2007
    Metadata
    Show full item record
    Abstract
    The glycosyltransferase enzymes (Lgts) responsible for the biosynthesis of the lipooligosaccharide-derived oligosaccharide structures from Moraxella catarrhalis have been investigated. This upper respiratory tract pathogen is responsible for a spectrum of illnesses, including otitis media (middle ear infection) in children, and contributes to exacerbations of chronic obstructive pulmonary disease in elderly patients. To investigate the function of the glycosyltransferase enzymes involved in the biosynthesis of lipooligosaccharide of M. catarrhalis and to gain some insight into the mechanism of serotype specificity for this ...
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    The glycosyltransferase enzymes (Lgts) responsible for the biosynthesis of the lipooligosaccharide-derived oligosaccharide structures from Moraxella catarrhalis have been investigated. This upper respiratory tract pathogen is responsible for a spectrum of illnesses, including otitis media (middle ear infection) in children, and contributes to exacerbations of chronic obstructive pulmonary disease in elderly patients. To investigate the function of the glycosyltransferase enzymes involved in the biosynthesis of lipooligosaccharide of M. catarrhalis and to gain some insight into the mechanism of serotype specificity for this microorganism, mutant strains of M. catarrhalis were produced. Examination by NMR and MS of the oligosaccharide structures produced by double-mutant strains (2951lgt1/4? and 2951lgt5/4?) and a single-mutant strain (2951lgt2?) of the bacterium has allowed us to propose a model for the serotype-specific expression of lipooligosaccharide in M. catarrhalis. According to this model, the presence/absence of Lgt4 and the Lgt2 allele determines the lipooligosaccharide structure produced by a strain. Furthermore, it is concluded that Lgt4 functions as an N-acetylglucosylamine transferase responsible for the addition of an a-d-GlcNAc (1?2) glycosidic linkage to the (1?4) branch, and also that there is competition between the glycosyltransferases Lgt1 and Lgt4. That is, in the presence of an active Lgt4, GlcNAc is preferentially added to the (1?4) chain of the growing oligosaccharide, instead of Glc. In serotype B strains, which lack Lgt4, Lgt1 adds a Glc at this position. This implies that active Lgt4 has a much higher affinity/specificity for the ߭(1?4)-linked Glc on the (1?4) branch than does Lgt1.
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    Journal Title
    The FEBS journal
    Volume
    274
    Publisher URI
    http://www.febsjournal.org/
    DOI
    https://doi.org/10.1111/j.1742-4658.2007.05746.x
    Copyright Statement
    © 2007 Wiley-Blackwell Publishing. The definitive version is available at www.interscience.wiley.com
    Subject
    Medicinal and biomolecular chemistry
    Biochemistry and cell biology
    Medical biochemistry and metabolomics
    Publication URI
    http://hdl.handle.net/10072/17699
    Collection
    • Journal articles

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