Phylogeny and Properties of a Novel Lectin Family with β-Trefoil Folding in Mussels

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  • Fujii Yuki
    Department of Pharmaceutical Sciences, Nagasaki International University
  • Gerdol Marco
    Department of Life Sciences, University of Trieste
  • Hasan Imtiaj
    Department of Life and Environmental System Science, Yokohama City University Department of Biochemistry and Molecular Biology, University of Rajshahi
  • Koide Yasuhiro
    Department of Life and Environmental System Science, Yokohama City University
  • Matsuzaki Risa
    Department of Life and Environmental System Science, Yokohama City University
  • Ikeda Mayu
    Department of Life and Environmental System Science, Yokohama City University
  • Rajia Sultana
    Department of Life and Environmental System Science, Yokohama City University Department of Pharmacy, Faculty of Pharmacy, Varendra University
  • Ogawa Yukiko
    Department of Pharmaceutical Sciences, Nagasaki International University
  • Kawsar S. M. Abe
    Department of Life and Environmental System Science, Yokohama City University Department of Chemistry, Faculty of Science, University of Chittagong
  • Ozeki Yasuhiro
    Department of Life and Environmental System Science, Yokohama City University

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Other Title
  • 二枚貝イガイ科にみるβ-トレフォイル骨格レクチンの新系図
  • ニマイガイ イガイカ ニ ミル v-トレフォイル コッカク レクチン ノ シン ケイズ

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Abstract

<p>A novel lectin, termed “MytiLec,” was isolated and characterized from the mussel Mytilus galloprovincialis, an important food and environmental indicator species found in marine coastal areas worldwide. MytiLec binds to the sugar moiety of globotriose (Gb3), an α-galactoside, leading to apoptosis of Gb3-expressing Burkitt’s lymphoma cells. The amino acid sequence of MytiLec is unusual, but 3-dimensional structural analysis reveals the presence of β-trefoil fold, a well-known feature in “R-type” lectins, a family of galactose-binding proteins found in many types of organisms. To date, MytiLec has been found only in a few species of the mollusk family Mytilidae and the phylum Brachiopoda, which also express typical R-type lectins. In this minireview, we discuss: (i) possible reasons for the unusual coexistence of two distinct lectin families in the same animal family; (ii) structural models of MytiLec that are useful for design of lectins with improved anti-cancer properties; (iii) construction of “Mitsuba,” an artificial lectin based on MytiLec that has similar carbohydrate-binding activity but a more stable monomeric form; (iv) regulation of cell growth by MytiLec and related lectins through binding to glycans.</p>

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