Bacillus thuringiensis protein transfer between rootstock and scion of grafted poplar

Plant Biol (Stuttg). 2012 Sep;14(5):745-50. doi: 10.1111/j.1438-8677.2011.00555.x. Epub 2012 Feb 28.

Abstract

Bacillus thuringiensis (Bt) Cry1Ac protein is a toxin against different leaf-eating lepidopteran insects that attack poplar trees. In the present study, the mode of migration of the Bt-Cry1Ac protein within poplar grafts was investigated. Grafting was done using Pb29 (transgenic poplar 741 with cry1Ac genes), CC71 (transgenic poplar 741 with cry3A genes), non-transgenic poplar 741 and non-transgenic Populus tomentosa, either as scion or as rootstock. In order to detect migration of Bt-Cry1Ac protein from one portion of the graft union to different tissues in the grafted plant, ELISA analysis was employed to assess the content of Bt-Cry1Ac protein in the phloem, xylem, pith and leaves of the grafted poplar. To further verify migration of Bt-Cry1Ac protein, Clostera anachoreta larvae, which are susceptible to Bt-Cry1Ac protein, were fed leaves from the control graft (i.e., graft portion that originally did not contain Bt-Cry1Ac protein). The results showed that Bt-Cry1Ac protein was transported between rootstock and scion mainly through the phloem. Migration of Bt-Cry1Ac protein in the grafted union was also evidenced in that the leaves of the control graft did have a lethal effect on C. anachoreta larvae in laboratory feeding experiments.

Keywords: Clostera anachoreta; Cry1Ac protein; Populus; grafting; pest resistance; transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacillus thuringiensis / metabolism*
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / metabolism*
  • Endotoxins / metabolism*
  • Hemolysin Proteins / metabolism*
  • Larva / growth & development
  • Lepidoptera / physiology
  • Plant Leaves / metabolism
  • Plants, Genetically Modified
  • Populus / metabolism*
  • Protein Transport

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins
  • insecticidal crystal protein, Bacillus Thuringiensis