Pierisins and CARP-1: ADP-Ribosylation of DNA by ARTCs in Butterflies and Shellfish

  • Tsuyoshi Nakano
  • Azusa Takahashi-Nakaguchi
  • Masafumi Yamamoto
  • Masahiko Watanabe
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 384)


The cabbage butterfly, Pieris rapae, and related species possess a previously unknown ADP-ribosylating toxin, guanine specific ADP-ribosyltransferase. This enzyme toxin, known as pierisin, consists of enzymatic N-terminal domain and receptor-binding C-terminal domain, or typical AB-toxin structure. Pierisin efficiently transfers an ADP-ribosyl moiety to the N2 position of the guanine base of dsDNA. Receptors for pierisin are suggested to be the neutral glycosphingolipids, globotriaosylceramide (Gb3), and globotetraosylceramide (Gb4). This DNA-modifying toxin exhibits strong cytotoxicity and induces apoptosis in various human cell lines, which can be blocked by Bcl-2. Pierisin also produces detrimental effects on the eggs and larvae of the non-habitual parasitoids. In contrast, a natural parasitoid of the cabbage butterfly, Cotesia glomerata, was resistant to this toxin. The physiological role of pierisin in the butterfly is suggested to be a defense factor against parasitization by wasps. Other type of DNA ADP-ribosyltransferase is present in certain kinds of edible clams. For example, the CARP-1 protein found in Meretrix lamarckii consists of an enzymatic domain without a possible receptor-binding domain. Pierisin and CARP-1 are almost fully non-homologous at the amino acid sequence level, but other ADP-ribosyltransferases homologous to pierisin are present in different biological species such as eubacterium Streptomyces. Possible diverse physiological roles of the DNA ADP-ribosyltransferases are discussed.


P2X7 Receptor Activity Domain Hard Clam Lepidopteran Insect Guanine Residue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



Double-strand DNA






N-glycosidic cholera toxin-like-ADP-ribosyltransferase catalyzing mono-ADP-ribosylation



The authors thank Dr. Ken-Ichi Odagiri for giving us a copy of phylogenic tree drawing.


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Copyright information

© Springer International Publishing Switzerland 2014

Authors and Affiliations

  • Tsuyoshi Nakano
    • 1
    • 2
  • Azusa Takahashi-Nakaguchi
    • 3
  • Masafumi Yamamoto
    • 4
  • Masahiko Watanabe
    • 5
  1. 1.Division of Cancer Development SystemNational Cancer Center Research InstituteTokyoJapan
  2. 2.Central Research Laboratories, Sysmex CorporationKobeJapan
  3. 3.Medical Mycology Research CenterChiba UniversityChibaJapan
  4. 4.Laboratory Animal Research DepartmentCentral Institute for Experimental AnimalsKawasakiJapan
  5. 5.School of PharmacyShujitsu UniversityOkayamaJapan

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