Identification of<i>Bombyx mori</i>Midgut Receptor for<i>Bacillus thuringiensis</i>Insecticidal CryIA(a) Toxin

Nagamatsu, Yasunori; Toda, Satoshi; Yamaguchi, Fumihide; Ogo, Masashi; Kogure, Masato; Nakamura, Masahiro; Shibata, Yasuyo; Katsumoto, Tetsuo

doi:10.1271/bbb.62.718

Cited by 87 publications

(65 citation statements)

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“…In M. sexta, Ͼ250-fold molar excess of the peptide was required, whereas in B. mori a Ͼ750-fold molar excess was needed. This difference may be because the Bt-R 175 -Cry1Aa toxin interaction depends on a native receptor conformation, since Cry1Aa binding to Bt-R 175 could not be detected under denaturing conditions (16,17). In contrast, M. sexta Bt-R 1 binds Cry1A toxins in both native and denaturing conditions (15).…”

Section: Discussionmentioning

confidence: 99%

“…In Manduca sexta, Cry1Aa, Cry1Ab, and Cry1Ac proteins bind to a 120-kDa aminopeptidase N (APN) (11)(12)(13) and to a 210-kDa cadherin-like protein (Bt-R 1 ) (14,15). In Bombyx mori, Cry1Aa binds to a 175-kDa cadherin-like protein (Bt-R 175 ) (16,17) and to a 120-kDa APN (18). In Heliothis virescens, Cry1Ac binds to two proteins of 120 and 170 kDa, both identified as APN (20,21).…”

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confidence: 99%

“…In Plutella xylostella and Lymantria dispar APNs were identified as Cry1Ac receptors (11,(22)(23)(24). All of these receptor molecule proteins are glycosylated (12,15,16,19). The interaction between toxin and its receptor can be complex.…”

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confidence: 99%

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Mapping the Epitope in Cadherin-like Receptors Involved inBacillus thuringiensis Cry1A Toxin Interaction Using Phage Display

Gómez¹,

Oltean²,

Gill³

et al. 2001

Journal of Biological Chemistry

134

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In susceptible lepidopteran insects, aminopeptidase N and cadherin-like proteins are the putative receptors for Bacillus thuringiensis (Bt) toxins. Using phage display, we identified a key epitope that is involved in toxin-receptor interaction. Three different scFv molecules that bind Cry1Ab toxin were obtained, and these scFv proteins have different amino acid sequences in the complementary determinant region 3 (CDR3). Binding analysis of these scFv molecules to different members of the Cry1A toxin family and to Escherichia coli clones expressing different Cry1A toxin domains showed that the three selected scFv molecules recognized only domain II. Heterologous binding competition of Cry1Ab toxin to midgut membrane vesicles from susceptible Manduca sexta larvae using the selected scFv molecules showed that scFv73 competed with Cry1Ab binding to the receptor. The calculated binding affinities (K d ) of scFv73 to Cry1Aa, Cry1Ab, and Cry1Ac toxins are in the range of 20 -51 nM. Sequence analysis showed this scFv73 molecule has a CDR3 significantly homologous to a region present in the cadherin-like protein from M. sexta (Bt-R 1 ), Bombyx mori (Bt-R 175 ), and Lymantria dispar. We demonstrated that peptides of 8 amino acids corresponding to the CDR3 from scFv73 or to the corresponding regions of Bt-R 1 or Bt-R 175 are also able to compete with the binding of Cry1Ab and Cry1Aa toxins to the Bt-R 1 or Bt-R 175 receptors. Finally, we showed that synthetic peptides homologous to Bt-R 1 and scFv73 CDR3 and the scFv73 antibody decreased the in vivo toxicity of Cry1Ab to M. sexta larvae. These results show that we have identified the amino acid region of Bt-R 1 and Bt-R 175 involved in Cry1A toxin interaction.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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Mapping the Epitope in Cadherin-like Receptors Involved inBacillus thuringiensis Cry1A Toxin Interaction Using Phage Display

Gómez¹,

Oltean²,

Gill³

et al. 2001

Journal of Biological Chemistry

134

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“…1). Protein Database (PDB) search with PredictProtein (Rost, 1996) demonstrated high similarity (S) and identity (IDE) of the putative O. nubilalis peptide to B. mori BtR175 (S ¼ 73%, IDE ¼ 61%; Nagamatsu et al, 1998b), Vadlamudi et al, 1995) and H. virescens BtR-4 (S ¼ 58%, IDE ¼ 72%; Gahan et al, 2001). A parsimony-based phylogeny used a consensus 3048 amino acid alignment of 12 lepidopteran cadherins including O. nubilalis and indicated three main divisions: cadherins from superfamilies Noctuoidae, Bombycoidae, Sphingoidea, and Pyraloidea and Gelchioidea (Fig.…”

Section: O Nubilalis Cadherin Identificationmentioning

confidence: 99%

Sequence variation in the cadherin gene of Ostrinia nubilalis: a tool for field monitoring

Coates

Sumerford

Hellmich

et al. 2005

Insect Biochemistry and Molecular Biology

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“…Two membrane proteins, cadherin and aminopeptidase-N (APN), have been implicated as possible receptors to insecticidal proteins. The putative receptor molecules have been cloned, heterologously expressed, and have been shown to bind Cry1A proteins by ligand blot analysis (4)(5)(6)(7)(8)(9)(10)(11). Although functional proof for cadherin as a Cry1A protein receptor has been demonstrated by cytolysis of insect cells expressing lepidopteran cadherin genes on exposure to Cry1Ab/Cry1Aa (10,12,13), a similar characterization of APN-Cry1A interaction has not been investigated yet.…”

mentioning

confidence: 99%

Knockdown of Aminopeptidase-N from Helicoverpa armigera Larvae and in Transfected Sf21 Cells by RNA Interference Reveals Its Functional Interaction with Bacillus thuringiensis Insecticidal Protein Cry1Ac

Swaminathan¹,

Rajagopal²,

Venkatesh

et al. 2007

Journal of Biological Chemistry

112

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Identification ofBombyx moriMidgut Receptor forBacillus thuringiensisInsecticidal CryIA(a) Toxin

Cited by 87 publications

References 1 publication

Mapping the Epitope in Cadherin-like Receptors Involved inBacillus thuringiensis Cry1A Toxin Interaction Using Phage Display

Mapping the Epitope in Cadherin-like Receptors Involved inBacillus thuringiensis Cry1A Toxin Interaction Using Phage Display

Sequence variation in the cadherin gene of Ostrinia nubilalis: a tool for field monitoring

Knockdown of Aminopeptidase-N from Helicoverpa armigera Larvae and in Transfected Sf21 Cells by RNA Interference Reveals Its Functional Interaction with Bacillus thuringiensis Insecticidal Protein Cry1Ac

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