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Chaperonin turned insect toxin

Author

Listed:
  • Naofumi Yoshida

    (Faculty of Agriculture, Kinki University)

  • Kenji Oeda

    (Agricultural Chemicals Research Laboratory)

  • Eijiro Watanabe

    (Genomic Science Laboratories, Sumitomo Pharmaceuticals)

  • Toshiyuki Mikami

    (Genomic Science Laboratories, Sumitomo Pharmaceuticals)

  • Yoshikazu Fukita

    (Organic Synthesis Research Laboratory, Sumitomo Chemical Co.)

  • Keiichiro Nishimura

    (Research Institute for Advanced Science and Technology, Osaka Prefecture University)

  • Koichiro Komai

    (Faculty of Agriculture, Kinki University)

  • Kazuhiko Matsuda

    (Faculty of Agriculture, Kinki University)

Abstract

Antlions are larvae of the Myrmeleontidae family that live on other insects1 by sucking out the body fluid from their prey, after first paralysing it with a toxin produced by salivary bacteria. Here we show that the paralysing toxin produced by bacterial endosymbionts in the saliva of Myrmeleon bore larvae is a homologue of GroEL, a protective heat-shock protein known as a molecular chaperone. The amino-acid residues critical for this protein's toxicity are located away from the regions essential to its protein-folding activity, indicating that the dual function of this GroEL homologue may benefit both the antlion and the endosymbiont.

Suggested Citation

  • Naofumi Yoshida & Kenji Oeda & Eijiro Watanabe & Toshiyuki Mikami & Yoshikazu Fukita & Keiichiro Nishimura & Koichiro Komai & Kazuhiko Matsuda, 2001. "Chaperonin turned insect toxin," Nature, Nature, vol. 411(6833), pages 44-44, May.
    • Handle: RePEc:nat:nature:v:411:y:2001:i:6833:d:10.1038_35075148
    DOI: 10.1038/35075148
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