Chaperonin turned insect toxin

Antlions are larvae of the Myrmeleontidae family that live on other insects 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...

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Bibliographic Details
Published inNature (London) Vol. 411; no. 6833; p. 44
Main Authors YOSHIDA, Naofumi, OEDA, Kenji, WATANABE, Eijiro, MIKAMI, Toshiyuki, FUKITA, Yoshikazu, NISHIMURA, Keiichiro, KOMAI, Koichiro, MATSUDA, Kazuhiko
Format Journal Article
LanguageEnglish
Published London Nature Publishing 03.05.2001
Subjects
Bacteriology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
GroEL protein
Microbiology
Myrmeleon bore
Myrmeleontidae
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Symbionte
Insecta
Chaperone
Enterobacter aerogenes
Neuroptera
Toxin
Arthropoda
Myrmeleontidae
Heat shock protein
Bacteria
Paralysis
Invertebrata
Enterobacteriaceae
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Summary:Antlions are larvae of the Myrmeleontidae family that live on other insects 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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
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ISSN:0028-0836
1476-4687
DOI:10.1038/35075148