Identification and Evolution of Venom Phospholipase A<sub>2</sub>Inhibitors from<i>Protobothrops elegans</i>Serum

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  • SO Shuhei
    Department of Applied Life Science, Faculty of Bioscience and Biotechnology, Sojo University
  • MURAKAMI Tatsuo
    Department of Applied Life Science, Faculty of Bioscience and Biotechnology, Sojo University
  • IKEDA Naoki
    Department of Applied Life Science, Faculty of Bioscience and Biotechnology, Sojo University
  • CHIJIWA Takahito
    Department of Applied Life Science, Faculty of Bioscience and Biotechnology, Sojo University
  • ODA-UEDA Naoko
    Department of Biochemistry, Faculty of Pharmaceutical Sciences, Sojo University
  • KURAISHI Takeshi
    Institute of Medical Science, The University of Tokyo
  • HATTORI Shosaku
    Institute of Medical Science, The University of Tokyo
  • OHNO Motonori
    Department of Applied Life Science, Faculty of Bioscience and Biotechnology, Sojo University

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タイトル別名
  • Identification and Evolution of Venom Phospholipase A2 Inhibitors from Protobothrops elegans Serum

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The cDNAs encoding venom phospholipase A2 (PLA2) inhibitors (PLIs), named Protobothrops elegans (Pe)γPLI-A, PeγPLI-B, PeαPLI-A, and PeαPLI-B, were cloned from the P. elegans liver cDNA library. They were further divided into several constituents due to nucleotide substitutions in their open reading frames. For PeαPLI-A, two constituents, PeαPLI-Aa and PeαPLI-Ab, were identified due to three nonsynonymous substitutions in exon 3. Far-western blot and mass-spectrometry analysis of the P. elegans serum proteins showed the presence of γPLIs, and αPLIs, which can bind venom PLA2s. In αPLIs from Protobothrops sera, A or B subtype-specific amino acid substitutions are concentrated only in exon 3. A comparison of γPLIs showed that γPLI-As are conserved and γPLI-Bs diversified. Mathematical analysis of the nucleotide sequences of Protobothrops γPLI-B cDNAs revealed that the particular loops in the three-finger motifs diversified by accelerated evolution. Such evolutionary features should have made serum PLIs acquire their respective inhibitory activities to adapt to venom PLA2 isozymes.

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