Function and Role of ATP-Binding Cassette Transporters as Receptors for 3D-Cry Toxins.

ABSTRACT: When ABC transporter family C2 (ABCC2) and ABC transporter family B1 (ABCB1) were heterologously expressed in non-susceptible cultured cells, the cells swelled in response to Cry1A and Cry3 toxins, respectively. Consistent with the notion that 3D-Cry toxins form cation-permeable pores, Bombyx mori ABCC2 (BmABCC2) facilitated cation-permeable pore formation by Cry1A when expressed in Xenopus oocytes. Furthermore, BmABCC2 had a high binding affinity (K_D) to Cry1Aa of 3.1 × 10^-10 M. These findings suggest that ABC transporters, including ABCC2 and ABCB1, are functional receptors for 3D-Cry toxins. In addition, the Cry2 toxins most distant from Cry1A toxins on the phylogenetic tree used ABC transporter A2 as a receptor. These data suggest that 3D-Cry

SUBMITTER: Sato R 

PROVIDER: S-EPMC6409751 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature