9 results match your criteria bmabcc2

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

FEBS J 2021 Oct 7. Epub 2021 Oct 7.

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Koganei, Japan.

Little information is available regarding the region of Cry toxins involved in binding to their major receptors, the ATP-binding cassette (ABC) transporters. We analyzed which Cry1Aa amino acid residues contribute to binding to Bombyx mori ABC transporter C2 (BmABCC2). Several two oxidized double-cysteine substitution mutant toxins were made. Read More

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October 2021

ATP-binding cassette transporter subfamily C members 2, 3 and cadherin protein are susceptibility-determining factors in Bombyx mori for multiple Bacillus thuringiensis Cry1 toxins.

Insect Biochem Mol Biol 2021 12 22;139:103649. Epub 2021 Sep 22.

Institute of Agrobiological Sciences, NARO, 1-2 Ohwashi, Tsukuba, Ibaraki 305-8634, Japan. Electronic address:

Field-evolved resistance of insect pests to Bacillus thuringiensis (Bt) toxins (Cry toxins) is a threat to the efficacy of Bt-based bio-insecticides and transgenic crops. Recent reports have suggested that ATP-binding cassette transporter subfamily C2 (ABCC2) and cadherin-like receptor play important roles in conferring susceptibility to Cry1 toxins. However, the receptors involved in Bt susceptibility in each insect remain unclear. Read More

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December 2021

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

Toxins (Basel) 2019 02 19;11(2). Epub 2019 Feb 19.

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Naka 2-24-16, Koganei, Tokyo 184-8588, Japan.

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, ABCC2 (BmABCC2) facilitated cation-permeable pore formation by Cry1A when expressed in oocytes. Furthermore, BmABCC2 had a high binding affinity () to Cry1Aa of 3. Read More

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February 2019

Extracellular loop structures in silkworm ABCC transporters determine their specificities for Cry toxins.

J Biol Chem 2018 06 17;293(22):8569-8577. Epub 2018 Apr 17.

From the Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan and

Cry toxins are insecticidal proteins used widely for pest control. They are lethal to a restricted range of insects via specific interactions with insect receptors such as the ABC transporter subfamily members C2 (ABCC2) and C3 (ABCC3). However, it is still unclear how these different receptors contribute to insect susceptibility to Cry1A toxins. Read More

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

Insect Biochem Mol Biol 2017 12 8;91:44-54. Epub 2017 Nov 8.

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Naka 2-24-16, Koganei, Tokyo 184-8588, Japan. Electronic address:

Because Bombyx mori ABC transporter C2 (BmABCC2) has 1000-fold higher potential than B. mori cadherin-like protein as a receptor for Bacillus thuringiensis Cry1Aa toxin (Tanaka et al., 2013), the gate-opening ability of the latent pore under six extracellular loops (ECLs) of BmABCC2 was expected to be the reason for its higher potential (Heckel, 2012). Read More

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December 2017

The domain II loops of Bacillus thuringiensis Cry1Aa form an overlapping interaction site for two Bombyx mori larvae functional receptors, ABC transporter C2 and cadherin-like receptor.

Biochim Biophys Acta Proteins Proteom 2017 Feb 23;1865(2):220-231. Epub 2016 Nov 23.

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Japan. Electronic address:

Information about the receptor-interaction region of Cry toxins, insecticidal proteins produced by Bacillus thuringiensis, is needed to elucidate the mode of action of Cry toxins and improve their toxicity through protein engineering. We analyzed the interaction sites on Cry1Aa with ABC transporter C2 (ABCC2), one of the most important Cry1A toxin receptors. A competitive binding assay revealed that the Bombyx mori ABCC2 (BmABCC2) Cry1A binding site was the same as the BtR175 binding site, suggesting that the loop region of Cry1Aa domain II is a binding site. Read More

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February 2017

Functional characterization of Bacillus thuringiensis Cry toxin receptors explains resistance in insects.

FEBS J 2016 12 29;283(24):4474-4490. Epub 2016 Nov 29.

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Japan.

Bacillus thuringiensis produces Cry toxins, which are used as insecticides in sprays and in transgenic crops. However, little is known about the function of Cry toxin receptors and the mechanisms that determine their binding specificity and activity. In this study, the cRNAs of Bombyx mori ABC transporter C2 (BmABCC2), the toxin-binding region of cadherin-like receptor (BtR175-TBR), or aminopeptidase N1 (BmAPN1) were injected into Xenopus oocytes, and the Cry1Aa-dependent cation-selective pore formation activities of these receptors were analyzed using a two-electrode voltage clamp. Read More

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December 2016

Single amino acid insertions in extracellular loop 2 of Bombyx mori ABCC2 disrupt its receptor function for Bacillus thuringiensis Cry1Ab and Cry1Ac but not Cry1Aa toxins.

Peptides 2016 Apr 27;78:99-108. Epub 2016 Feb 27.

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo, Japan. Electronic address:

In a previous report, seven Cry1Ab-resistant strains were identified in the silkworm, Bombyx mori; these strains were shown to have a tyrosine insertion at position 234 in extracellular loop 2 of the ABC transporter C2 (BmABCC2). This insertion was confirmed to destroy the receptor function of BmABCC2 and confer the strains resistance against Cry1Ab and Cry1Ac. However, these strains were susceptible to Cry1Aa. Read More

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The ATP-binding cassette transporter subfamily C member 2 in Bombyx mori larvae is a functional receptor for Cry toxins from Bacillus thuringiensis.

FEBS J 2013 Apr 14;280(8):1782-94. Epub 2013 Mar 14.

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Japan.

Bacillus thuringiensis is the most widely used biopesticide, and its Cry toxin genes are essential transgenes for the generation of insect-resistant transgenic crops. Recent reports have suggested that ATP-binding cassette transporter subfamily C2 (ABCC2) proteins are implicated in Cry intoxication, and that a single amino acid insertion results in high levels of resistance to Cry1 toxins. However, there is currently no available direct evidence of functional interactions between ABCC2 and Cry toxins. Read More

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