Partial characterization of oligosaccharides expressed on midgut microvillar glycoproteins of the mosquito, Anopheles stephensi Liston

S. Wilkins, Peter Francis Billingsley

    Research output: Contribution to journalArticle

    30 Citations (Scopus)

    Abstract

    Midguts of the malaria-transmitting mosquito, Anopheles stephensi, were homogenized and microvillar membranes prepared by calcium precipitation and differential centrifugation. Oligosaccharides present on the microvillar glycoproteins were identified by lectin blotting before and after in vitro and in situ treatments with endo- and exo-glycosidases. Twenty-eight glycoproteins expressed a structurally restricted range of terminal sugars and oligosaccharide linkages. Twenty-three glycoproteins expressed oligomannose and/or hybrid N-linked oligosaccharides, some with alpha1-6 linked fucose as a core residue. Complex-type N-linked oligosaccharides on eight glycoproteins all possessed terminal N-acetylglucosamine, and alpha- and beta -linked N-acetylgalactosamine. Eight glycoproteins expressed O-linked oligosaccharides all containing N-acetylgalactosamine with or without further substitutions of fucose and/or galactose. Galactose beta1-3/4/6N-acetylglucosamine-, sialic acid alpha2-3/6galactose-, fucosea1-2galactose- and galactoseal-3galactose-were not detected. Terminal a-linked N-acetylgalactosamine residues on N-linked oligosaccharides are described for the first time in insects. The nature and function of these midgut glycoproteins have yet to be identified. but the oligosaccharide side chains are candidate receptors for ookinete binding and candidate targets for transmission blocking strategies (C) 2001 Elsevier Science Ltd. All rights reserved.

    Original languageEnglish
    Pages (from-to)937-948
    Number of pages11
    JournalInsect Biochemistry and Molecular Biology
    Volume31
    DOIs
    Publication statusPublished - 2001

    Keywords

    • mosquito
    • midgut
    • microvilli
    • glycoproteins
    • oligosaccharide
    • BETA-N-ACETYLGLUCOSAMINIDASE
    • ASN-LINKED OLIGOSACCHARIDES
    • WHEAT-GERM AGGLUTININ
    • AEDES-AEGYPTI
    • DIPLOCOCCUS-PNEUMONIAE
    • COMBINING SITE
    • SUGAR CHAINS
    • SIALIC-ACID
    • PURIFICATION
    • SPECIFICITY

    Cite this

    Partial characterization of oligosaccharides expressed on midgut microvillar glycoproteins of the mosquito, Anopheles stephensi Liston. / Wilkins, S.; Billingsley, Peter Francis.

    In: Insect Biochemistry and Molecular Biology, Vol. 31, 2001, p. 937-948.

    Research output: Contribution to journalArticle

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    abstract = "Midguts of the malaria-transmitting mosquito, Anopheles stephensi, were homogenized and microvillar membranes prepared by calcium precipitation and differential centrifugation. Oligosaccharides present on the microvillar glycoproteins were identified by lectin blotting before and after in vitro and in situ treatments with endo- and exo-glycosidases. Twenty-eight glycoproteins expressed a structurally restricted range of terminal sugars and oligosaccharide linkages. Twenty-three glycoproteins expressed oligomannose and/or hybrid N-linked oligosaccharides, some with alpha1-6 linked fucose as a core residue. Complex-type N-linked oligosaccharides on eight glycoproteins all possessed terminal N-acetylglucosamine, and alpha- and beta -linked N-acetylgalactosamine. Eight glycoproteins expressed O-linked oligosaccharides all containing N-acetylgalactosamine with or without further substitutions of fucose and/or galactose. Galactose beta1-3/4/6N-acetylglucosamine-, sialic acid alpha2-3/6galactose-, fucosea1-2galactose- and galactoseal-3galactose-were not detected. Terminal a-linked N-acetylgalactosamine residues on N-linked oligosaccharides are described for the first time in insects. The nature and function of these midgut glycoproteins have yet to be identified. but the oligosaccharide side chains are candidate receptors for ookinete binding and candidate targets for transmission blocking strategies (C) 2001 Elsevier Science Ltd. All rights reserved.",
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    AB - Midguts of the malaria-transmitting mosquito, Anopheles stephensi, were homogenized and microvillar membranes prepared by calcium precipitation and differential centrifugation. Oligosaccharides present on the microvillar glycoproteins were identified by lectin blotting before and after in vitro and in situ treatments with endo- and exo-glycosidases. Twenty-eight glycoproteins expressed a structurally restricted range of terminal sugars and oligosaccharide linkages. Twenty-three glycoproteins expressed oligomannose and/or hybrid N-linked oligosaccharides, some with alpha1-6 linked fucose as a core residue. Complex-type N-linked oligosaccharides on eight glycoproteins all possessed terminal N-acetylglucosamine, and alpha- and beta -linked N-acetylgalactosamine. Eight glycoproteins expressed O-linked oligosaccharides all containing N-acetylgalactosamine with or without further substitutions of fucose and/or galactose. Galactose beta1-3/4/6N-acetylglucosamine-, sialic acid alpha2-3/6galactose-, fucosea1-2galactose- and galactoseal-3galactose-were not detected. Terminal a-linked N-acetylgalactosamine residues on N-linked oligosaccharides are described for the first time in insects. The nature and function of these midgut glycoproteins have yet to be identified. but the oligosaccharide side chains are candidate receptors for ookinete binding and candidate targets for transmission blocking strategies (C) 2001 Elsevier Science Ltd. All rights reserved.

    KW - mosquito

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    KW - microvilli

    KW - glycoproteins

    KW - oligosaccharide

    KW - BETA-N-ACETYLGLUCOSAMINIDASE

    KW - ASN-LINKED OLIGOSACCHARIDES

    KW - WHEAT-GERM AGGLUTININ

    KW - AEDES-AEGYPTI

    KW - DIPLOCOCCUS-PNEUMONIAE

    KW - COMBINING SITE

    KW - SUGAR CHAINS

    KW - SIALIC-ACID

    KW - PURIFICATION

    KW - SPECIFICITY

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    DO - 10.1016/S0965-1748(01)00040-6

    M3 - Article

    VL - 31

    SP - 937

    EP - 948

    JO - Insect Biochemistry and Molecular Biology

    JF - Insect Biochemistry and Molecular Biology

    SN - 0965-1748

    ER -