The base and root of domain II loops of Cry toxins contribute to binding to Bombyx mori ABC transporter C2

FEBS Journal ◽  
2021 ◽  
Author(s):  
Satomi Adegawa ◽  
Naomi Yamaguchi ◽  
Ryoichi Sato
Keyword(s):  
Bombyx Mori ◽  
Abc Transporter ◽  
Cry Toxins

Binding of Phylogenetically Distant Bacillus thuringiensis Cry Toxins to a Bombyx mori Aminopeptidase N Suggests Importance of Cry Toxin's Conserved Structure in Receptor Binding

1999 ◽  
Vol 39 (1) ◽  
pp. 14-20 ◽  
Author(s):  
Ayaka Shinkawa ◽  
Katsuro Yaoi ◽  
Tomoyuki Kadotani ◽  
Morikazu Imamura ◽  
Nobuo Koizumi ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Bombyx Mori ◽  
Receptor Binding ◽  
Aminopeptidase N ◽  
Cry Toxins

Genome-wide analysis of the ATP-binding cassette (ABC) transporter gene family in the silkworm, Bombyx mori

2012 ◽  
Vol 39 (7) ◽  
pp. 7281-7291 ◽  
Author(s):  
Xiaodong Xie ◽  
Tingcai Cheng ◽  
Genhong Wang ◽  
Jun Duan ◽  
Weihuan Niu ◽  
...  
Keyword(s):  
Gene Family ◽  
Bombyx Mori ◽  
Abc Transporter ◽  
Atp Binding ◽  
Transporter Gene ◽  
Genome Wide Analysis ◽  
Genome Wide ◽  
Silkworm Bombyx Mori ◽  
Atp Binding Cassette

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

Toxins ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 124 ◽  
Author(s):  
Ryoichi Sato ◽  
Satomi Adegawa ◽  
Xiaoyi Li ◽  
Shiho Tanaka ◽  
Haruka Endo
Keyword(s):  
Abc Transporter ◽  
Abc Transporters ◽  
Cultured Cells ◽  
Cell Swelling ◽  
Cry Toxins ◽  
Transporter Family ◽  
Pore Opening ◽  
Synergistic Relationship ◽  
High Binding Affinity

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 (KD) 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 toxins use ABC transporters as receptors. In terms of inducing cell swelling, ABCC2 has greater activity than cadherin-like receptor. The pore opening of ABC transporters was hypothesized to be linked to their receptor function, but this was repudiated by experiments using mutants deficient in export activity. The synergistic relationship between ABCC2 and cadherin-like receptor explains their ability to cause resistance in one species of insect.

Bombyx mori ABC transporter C2 structures responsible for the receptor function of Bacillus thuringiensis Cry1Aa toxin

2017 ◽  
Vol 91 ◽  
pp. 44-54 ◽  
Author(s):  
Shiho Tanaka ◽  
Haruka Endo ◽  
Satomi Adegawa ◽  
Ami Iizuka ◽  
Kazuhiro Imamura ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Bombyx Mori ◽  
Abc Transporter ◽  
Receptor Function

scholarly journals ATP-Binding Cassette Subfamily a Member 2 Is a Functional Receptor for Bacillus thuringiensis Cry2A Toxins in Bombyx mori, But Not for Cry1A, Cry1C, Cry1D, Cry1F, or Cry9A Toxins

Toxins ◽  
2020 ◽  
Vol 12 (2) ◽  
pp. 104 ◽  
Author(s):  
Xiaoyi Li ◽  
Kazuhisa Miyamoto ◽  
Yoko Takasu ◽  
Sanae Wada ◽  
Tetsuya Iizuka ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Bombyx Mori ◽  
Cell Swelling ◽  
Cross Resistance ◽  
Atp Binding ◽  
Transcription Activator ◽  
Cry Toxins ◽  
Toxin Resistance ◽  
Functional Receptor ◽  
Atp Binding Cassette

Cry toxins are insecticidal proteins produced by Bacillus thuringiensis (Bt). They are used commercially to control insect pests since they are very active in specific insects and are harmless to the environment and human health. The gene encoding ATP-binding cassette subfamily A member 2 (ABCA2) was identified in an analysis of Cry2A toxin resistance genes. However, we do not have direct evidence for the role of ABCA2 for Cry2A toxins or why Cry2A toxin resistance does not cross to other Cry toxins. Therefore, we performed two experiments. First, we edited the ABCA2 sequence in Bombyx mori using transcription activator-like effector-nucleases (TALENs) and confirmed the susceptibility-determining ability in a diet overlay bioassay. Strains with C-terminal half-deleted BmABCA2 showed strong and specific resistance to Cry2A toxins; even strains carrying a deletion of 1 to 3 amino acids showed resistance. However, the C-terminal half-deleted strains did not show cross-resistance to other toxins. Second, we conducted a cell swelling assay and confirmed the specific ability of BmABCA2 to Cry2A toxins in HEK239T cells. Those demonstrated that BmABCA2 is a functional receptor for Cry2A toxins and that BmABCA2 deficiency-dependent Cry2A resistance does not confer cross-resistance to Cry1A, Cry1Ca, Cry1Da, Cry1Fa or Cry9Aa toxins.

Anti-diabetic effects of the silkworm (Bombyx mori.) extracts in the db/db mice

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
KS Ryu ◽  
HS Lee ◽  
KY Kim ◽  
MJ Kim ◽  
PD Kang ◽  
...  
Keyword(s):  
Bombyx Mori ◽  
Silkworm Bombyx Mori

LXR und ABC-Transporter-Expression im Trophoblasten bei IUGR

2017 ◽  
Vol 77 (04) ◽  
pp. 379-395
Author(s):  
L Schmieding ◽  
A Klein ◽  
N Maass ◽  
C Eckmann-Scholz ◽  
D Lütjohann ◽  
...  
Keyword(s):  
Abc Transporter ◽  
Transporter Expression
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