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Studies on molecular structures and oligosaccharide-binding specificities of algal lectins

Research Project

Project/Area Number 09460095
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field Fisheries chemistry
Research InstitutionFaculty of Applied Biological Science, Hiroshima University

Principal Investigator

HORI Kanji  Hiroshima University, Faculty of Applied Biological Science, Professor, 生物生産学部, 教授 (50116662)

Project Period (FY) 1997 – 1999
Project Status Completed (Fiscal Year 1999)
Budget Amount *help
¥10,300,000 (Direct Cost: ¥10,300,000)
Fiscal Year 1999: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1998: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1997: ¥6,700,000 (Direct Cost: ¥6,700,000)
Keywordslectins / marine algae / blue-green alga (cyanobacterium) / molecular structures / oligosaccharide / sugar binding specificity / sugar chains / amino acid sequence / 糖鎖認識 / 糖鎖認識ドメイン / 生物活性 / オリゴサッカライド
Research Abstract

The research results showed that the lectins from twelve algal species examined have the highly binding specificity to some definite structures of oligosaccharides such as high-mannose type, complex type, or both type of N-glycans, forssman antigen, or sialyl Lewis X, respectively. The high-mannose or complex type N-glycan specific lectins were further divided into several groups by the difference of the branched structures recognized. The lectins thus recognize the branched moiety of the N-glycans. Interestingly, however, the reducing terminal N-acetylchitobiose of the N-glycans was essential for the binding of these lectins to the glycans, because they did not bind to any of the branched oligosaccharides themselves. Thus these algal lectins had the rigid binding specificity for some oligosaccharide structures.
Among the high-mannose type N-glycan specific lectins, the complete primary structures of the lectins from the red alga Eucheuma serra and the blue-green alga Oscillatoria agard … More hii were determined. Both lectins had the very similar sequences to each other including the tandem repeat structures of homologous sequences of the N-terminal 67 amino acids. The number of the repeats was different between E.serra lectin (267 amino acids of 4 repeats) and O.agardhii lectin (132 amino acids of 2 repeats). On the other hand, the number of the repeats was well agreement with that of oligosaccharide-binding sites per a monomeric molecule for both lectins. The results indicate that a repeating unit corresponds to an oligosaccharide-recognition domain and the monomeric lectins agglutinate cells by having the multiple carbohydrate-binding sites on each single polypeptide chain. In homology search, surprisingly, the sequences of both algal lectins showed the very high similarity with that of a bacterium Myxococcus xanthus agglutinin including the four tandem repeats of the N-terminal 67 amino acids. Thus it found that a new lectin family having structural similarity was present among the lower organisms of the red alga, the blue-green alga (cyanobacterium) and the bacterium. This is the first example that the structural similarity of lectin molecules was found between prokaryote and eukaryote organisms. Less

Report

(4 results)
  • 1999 Annual Research Report   Final Research Report Summary
  • 1998 Annual Research Report
  • 1997 Annual Research Report
  • Research Products

    (10 results)

All Other

All Publications (10 results)

  • [Publications] 川久保 明宏: "The marine red alga Eucheuina serra T-Agardh, a high yielding source of two isolection"J.Appl.phycol. 9. 331-338 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] 川久保 明宏: "Occurrence of highly yielded lectins homologous within the genus Eucheuma"J.Appl.phycol. 11. 149-156 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] 佐藤雄一郎: "PuriFication and characterization of a new lectin from a freshasater Cyanobacterium Oscillaforia agarithii"Comp.Biochem.physiol.. 125B. 169-177 (2000)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] 堀 貫治: "Primery structures of two hemogglatinins from the marine red alga Hypnea japonica"Biochim.Biophys.Acta. 147. 226-236 (2000)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Kawakubo, A., Makino, H., Ohnishi, J., Hirohara, H.and Hori, K.: "The marine red alga Eucheuma serra J.Agardh, a high yielding source of two isolectins."J.Appl.Phycol.. 9. 331-338 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Kawakubo, A., Makino, H., Ohnishi, J., Hirohara, H.and Hori, K.: "Occurrence of highly yieldedlectins homologous within the genus Eucheuma."J.Appl.Phycol.. 11. 149-156 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Sato, Y., Murakami, M., Miyazawa, K.and Hori, K.: "Purification and characterization of a new lectin from a freshwater cyanobacteium, Oscillatoria agardhii."Comp.Biochem.Physiol.. 125B. 169-177 (2000)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Hori, K., Matsubara, K.and Miyazawa, K.: "Primary structures of two hemagglutinins from the marine red alga, Hypnea japonica."Biochim.Biophys.Acta.. 147. 226-236 (2000)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Sato,Y: "Purification and characterization of a new lectin from a freshwoter cyanabocterian,Oscillatoria agardhii"Comp.Biochem .physiol.. 125B. 169-177 (2000)

    • Related Report
      1999 Annual Research Report
  • [Publications] Hori,K: "Primary structures of two hemagglutinins from the marine red dgb,Hypnea japonica"Biochim.Biophys.Acta. (in press). (2000)

    • Related Report
      1999 Annual Research Report

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Published: 1997-04-01   Modified: 2016-04-21  

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