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Cry1A toxins of Bacillus thuringiensis bind specifically to a region adjacent to the membrane-proximal extracellular domain of BT-R(1) in Manduca sexta: involvement of a cadherin in the entomopathogenicity of Bacillus thuringiensis.
Insect Biochem Mol Biol. 2002 Sep; 32(9):1025-36.IB

Abstract

Many subspecies of the soil bacterium Bacillus thuringiensis produce various parasporal crystal proteins, also known as Cry toxins, that exhibit insecticidal activity upon binding to specific receptors in the midgut of susceptible insects. One such receptor, BT-R(1) (210 kDa), is a cadherin located in the midgut epithelium of the tobacco hornworm, Manduca sexta. It has a high binding affinity (K(d) approximately 1nM) for the Cry1A toxins of B. thuringiensis. Truncation analysis of BT-R(1) revealed that the only fragment capable of binding the Cry1A toxins of B. thuringiensis was a contiguous 169-amino acid sequence adjacent to the membrane-proximal extracellular domain. The purified toxin-binding fragment acted as an antagonist to Cry1Ab toxin by blocking the binding of toxin to the tobacco hornworm midgut and inhibiting insecticidal action. Exogenous Cry1Ab toxin bound to intact COS-7 cells expressing BT-R(1) cDNA, subsequently killing the cells. Recruitment of BT-R(1) by B. thuringiensis indicates that the bacterium interacts with a specific cell adhesion molecule during its pathogenesis. Apparently, Cry toxins, like other bacterial toxins, attack epithelial barriers by targeting cell adhesion molecules within susceptible insect hosts.

Authors+Show Affiliations

Dorsch JA
Center for Biotechnology and Bioinformatics, The University of Texas at Dallas, P.O. Box 830688, FO31, Richardson, TX 75083-0688, USA.
Candas M
No affiliation info available
Griko NB
No affiliation info available
Maaty WS
No affiliation info available
Midboe EG
No affiliation info available
Vadlamudi RK
No affiliation info available
Bulla LA
No affiliation info available

MeSH

Amino Acid SequenceAnimalsBacillus thuringiensisBacillus thuringiensis ToxinsBacterial ProteinsBacterial ToxinsBinding SitesCOS CellsCadherinsChlorocebus aethiopsEndotoxinsHemolysin ProteinsInsect ProteinsLarvaManducaMolecular Sequence DataProtein BindingProtein Structure, TertiaryReceptors, Cell SurfaceTransfection

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

12213239

Citation

Dorsch, J A., et al. "Cry1A Toxins of Bacillus Thuringiensis Bind Specifically to a Region Adjacent to the Membrane-proximal Extracellular Domain of BT-R(1) in Manduca Sexta: Involvement of a Cadherin in the Entomopathogenicity of Bacillus Thuringiensis." Insect Biochemistry and Molecular Biology, vol. 32, no. 9, 2002, pp. 1025-36.
Dorsch JA, Candas M, Griko NB, et al. Cry1A toxins of Bacillus thuringiensis bind specifically to a region adjacent to the membrane-proximal extracellular domain of BT-R(1) in Manduca sexta: involvement of a cadherin in the entomopathogenicity of Bacillus thuringiensis. Insect Biochem Mol Biol. 2002;32(9):1025-36.
Dorsch, J. A., Candas, M., Griko, N. B., Maaty, W. S., Midboe, E. G., Vadlamudi, R. K., & Bulla, L. A. (2002). Cry1A toxins of Bacillus thuringiensis bind specifically to a region adjacent to the membrane-proximal extracellular domain of BT-R(1) in Manduca sexta: involvement of a cadherin in the entomopathogenicity of Bacillus thuringiensis. Insect Biochemistry and Molecular Biology, 32(9), 1025-36.
Dorsch JA, et al. Cry1A Toxins of Bacillus Thuringiensis Bind Specifically to a Region Adjacent to the Membrane-proximal Extracellular Domain of BT-R(1) in Manduca Sexta: Involvement of a Cadherin in the Entomopathogenicity of Bacillus Thuringiensis. Insect Biochem Mol Biol. 2002;32(9):1025-36. PubMed PMID: 12213239.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cry1A toxins of Bacillus thuringiensis bind specifically to a region adjacent to the membrane-proximal extracellular domain of BT-R(1) in Manduca sexta: involvement of a cadherin in the entomopathogenicity of Bacillus thuringiensis. AU - Dorsch,J A, AU - Candas,M, AU - Griko,N B, AU - Maaty,W S A, AU - Midboe,E G, AU - Vadlamudi,R K, AU - Bulla,L A,Jr PY - 2002/9/6/pubmed PY - 2002/11/26/medline PY - 2002/9/6/entrez SP - 1025 EP - 36 JF - Insect biochemistry and molecular biology JO - Insect Biochem Mol Biol VL - 32 IS - 9 N2 - Many subspecies of the soil bacterium Bacillus thuringiensis produce various parasporal crystal proteins, also known as Cry toxins, that exhibit insecticidal activity upon binding to specific receptors in the midgut of susceptible insects. One such receptor, BT-R(1) (210 kDa), is a cadherin located in the midgut epithelium of the tobacco hornworm, Manduca sexta. It has a high binding affinity (K(d) approximately 1nM) for the Cry1A toxins of B. thuringiensis. Truncation analysis of BT-R(1) revealed that the only fragment capable of binding the Cry1A toxins of B. thuringiensis was a contiguous 169-amino acid sequence adjacent to the membrane-proximal extracellular domain. The purified toxin-binding fragment acted as an antagonist to Cry1Ab toxin by blocking the binding of toxin to the tobacco hornworm midgut and inhibiting insecticidal action. Exogenous Cry1Ab toxin bound to intact COS-7 cells expressing BT-R(1) cDNA, subsequently killing the cells. Recruitment of BT-R(1) by B. thuringiensis indicates that the bacterium interacts with a specific cell adhesion molecule during its pathogenesis. Apparently, Cry toxins, like other bacterial toxins, attack epithelial barriers by targeting cell adhesion molecules within susceptible insect hosts. SN - 0965-1748 UR - https://www.unboundmedicine.com/medline/citation/12213239/Cry1A_toxins_of_Bacillus_thuringiensis_bind_specifically_to_a_region_adjacent_to_the_membrane_proximal_extracellular_domain_of_BT_R_1__in_Manduca_sexta:_involvement_of_a_cadherin_in_the_entomopathogenicity_of_Bacillus_thuringiensis_ DB - PRIME DP - Unbound Medicine ER -
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