Cry1A toxins of Bacillus thuringiensis bind specifically to a region adjacent to the membrane-proximal extracellular domain of BT-R1 in Manduca sexta: Involvement of a cadherin in the-entomopathogenicity of Bacillus thuringiensis

J. A. Dorsch, M. Candas, N. B. Griko, W. S A Maaty, E. G. Midboe, Ratna K Vadlamudi, L. A. Bulla

Research output: Contribution to journalArticle

94 Citations (Scopus)

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-R1 (210 kDa), is a cadherin located in the midgut epithelium of the tobacco hornworm, Manduca sexta. It has a high binding affinity (Kd ∼ 1nM) for the Cry1A toxins of B. thuringiensis. Truncation analysis of BT-R1 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-R1 cDNA, subsequently killing the cells. Recruitment of BT-R1 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.

Original languageEnglish (US)
Pages (from-to)1025-1036
Number of pages12
JournalInsect Biochemistry and Molecular Biology
Volume32
Issue number9
DOIs
StatePublished - Sep 2002
Externally publishedYes

Fingerprint

Manduca
Bacillus thuringiensis
Tobacco
cadherins
Manduca sexta
Cell Adhesion Molecules
Bacilli
Cadherins
Bacteria
toxins
Membranes
Bacterial Toxins
Insects
Complementary DNA
Cells
midgut
Soils
Amino Acids
Crystals
COS Cells

Keywords

  • /BT-R
  • Bacillus thuringiensis
  • Cadherin
  • COS-7
  • Cry toxin
  • Entomopathogenicity
  • Insecticide
  • Integrin
  • Transfected cells
  • Transmembrane protein

ASJC Scopus subject areas

  • Insect Science
  • Biochemistry

Cite this

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title = "Cry1A toxins of Bacillus thuringiensis bind specifically to a region adjacent to the membrane-proximal extracellular domain of BT-R1 in Manduca sexta: Involvement of a cadherin in the-entomopathogenicity of Bacillus thuringiensis",
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-R1 (210 kDa), is a cadherin located in the midgut epithelium of the tobacco hornworm, Manduca sexta. It has a high binding affinity (Kd ∼ 1nM) for the Cry1A toxins of B. thuringiensis. Truncation analysis of BT-R1 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-R1 cDNA, subsequently killing the cells. Recruitment of BT-R1 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.",
keywords = "/BT-R, Bacillus thuringiensis, Cadherin, COS-7, Cry toxin, Entomopathogenicity, Insecticide, Integrin, Transfected cells, Transmembrane protein",
author = "Dorsch, {J. A.} and M. Candas and Griko, {N. B.} and Maaty, {W. S A} and Midboe, {E. G.} and Vadlamudi, {Ratna K} and Bulla, {L. A.}",
year = "2002",
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T1 - Cry1A toxins of Bacillus thuringiensis bind specifically to a region adjacent to the membrane-proximal extracellular domain of BT-R1 in Manduca sexta

T2 - 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, Ratna K

AU - Bulla, L. A.

PY - 2002/9

Y1 - 2002/9

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-R1 (210 kDa), is a cadherin located in the midgut epithelium of the tobacco hornworm, Manduca sexta. It has a high binding affinity (Kd ∼ 1nM) for the Cry1A toxins of B. thuringiensis. Truncation analysis of BT-R1 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-R1 cDNA, subsequently killing the cells. Recruitment of BT-R1 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.

AB - 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-R1 (210 kDa), is a cadherin located in the midgut epithelium of the tobacco hornworm, Manduca sexta. It has a high binding affinity (Kd ∼ 1nM) for the Cry1A toxins of B. thuringiensis. Truncation analysis of BT-R1 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-R1 cDNA, subsequently killing the cells. Recruitment of BT-R1 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.

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KW - Integrin

KW - Transfected cells

KW - Transmembrane protein

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