Proteomic identification of Bacillus thuringiensis subsp. israelensis toxin Cry4Ba binding proteins in midgut membranes from Aedes (Stegomyia) aegypti Linnaeus (Diptera, Culicidae) larvae

Bayyareddy, Krishnareddy; Andacht, Tracy M.; Abdullah, Mohd Amir F.; Adang, Michael J.

doi:10.1016/j.ibmb.2009.01.002

Cited by 75 publications

(98 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…aegypti BBMV. A number of studies showed the interaction of Cry11Aa or Cry4Ba toxins with mosquito BBMV (5,17,20). Toxin affinity to BBMV has been measured with Cry11Aa, Cry4Aa and Cry4Ba, Cry1C, and the binary toxin from B. sphaericus (2,3,14,33,34).…”

Section: Resultsmentioning

confidence: 99%

Cadherin, Alkaline Phosphatase, and Aminopeptidase N as Receptors of Cry11Ba Toxin from Bacillus thuringiensis subsp. jegathesan in Aedes aegypti

Likitvivatanavong

Chen

Bravo

et al. 2011

Appl Environ Microbiol

View full text Add to dashboard Cite

Cry11Ba is one of the most toxic proteins to mosquito larvae produced by Bacillus thuringiensis. It binds Aedes aegypti brush border membrane vesicles (BBMV) with high affinity, showing an apparent dissociation constant (K d ) of 8.2 nM. We previously reported that an anticadherin antibody competes with Cry11Ba binding to BBMV, suggesting a possible role of cadherin as a toxin receptor. Here we provide evidence of specific cadherin repeat regions involved in this interaction. Using cadherin fragments as competitors, a C-terminal fragment which contains cadherin repeat 7 (CR7) to CR11 competed with Cry11Ba binding to BBMV. This binding was also efficiently competed by the CR9, CR10, and CR11 peptide fragments. Moreover, we show CR11 to be an important region of interaction with Cry11Ba toxin. An alkaline phosphatase (AaeALP1) and an aminopeptidase-N (AaeAPN1) also competed with Cry11Ba binding to Ae. aegypti BBMV. Finally, we found that Cry11Ba and Cry4Ba share binding sites. Synthetic peptides corresponding to loops ␣8, ␤2-␤3 (loop 1), ␤8-␤9, and ␤10-␤11 (loop 3) of Cry4Ba compete with Cry11Ba binding to BBMV, suggesting Cry11Ba and Cry4Ba have common sites involved in binding Ae. aegypti BBMV. The data suggest that three different Ae. aegypti midgut proteins, i.e., cadherin, AaeALP1, and AaeAPN1, are involved in Cry11Ba binding to Ae. aegypti midgut brush border membranes.

show abstract

Section: Resultsmentioning

confidence: 99%

Cadherin, Alkaline Phosphatase, and Aminopeptidase N as Receptors of Cry11Ba Toxin from Bacillus thuringiensis subsp. jegathesan in Aedes aegypti

Likitvivatanavong

Chen

Bravo

et al. 2011

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…Among them are actin and V-ATP-synthase in Lepidoptera (18 -20) and Diptera (21), heat shock cognate protein in Lepidoptera (20), and flotillin and prohibitin in Diptera (21). Actin, V-ATP-synthase, and prohibitin have been also identified as Cry binding partners in Coleoptera through targeted mass spectrometry protein analysis.…”

mentioning

confidence: 99%

Sodium Solute Symporter and Cadherin Proteins Act as Bacillus thuringiensis Cry3Ba Toxin Functional Receptors in Tribolium castaneum

Contreras

Schoppmeier

Real

et al. 2013

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Interaction with insect midgut receptors is required for Bacillus thuringienesis (Bt) toxicity. Results: RNAi knockdown of E-cadherin and sodium solute symporter (SSS) genes dramatically decreases Tribolium castaneum (Tc) larval susceptibility to Cry3Ba. A SSS fragment enhances Cry3Ba toxicity. Conclusion: E-cadherin and SSS but not aminopeptidase N are Cry3Ba receptors in Tc. Significance: For the first time, SSS was demonstrated as a Bt functional receptor.

show abstract

“…Furthermore, a series of other proteins, i.e. aminopeptidase, several alkaline phosphatase isoforms, flotillin, prohibitin, V-ATPase B subunit and actin were shown to bind Cry4Ba in Aedes aegypti (Bayyareddy et al, 2009). Data are also available on the membrane receptors of Cry11Aa.…”

Section: Pesticides In the Modern World -Pests Control And Pesticidesmentioning

confidence: 99%

“…The specific receptors of Bti toxins in mosquito midguts have been much less studied. To date, one cadherin was identified as Cry4B receptor and one APN as Cry11B receptor in Anopheles Abdullah et al, 2006;Zhang et al, 2008), and one cadherin as Cry11B receptor, one APN as Cry11A receptor and one other ALP as Cry4B receptor in Aedes (Chen et al, 2009a, Fernandez-Luna et al, 2006, Bayyareddy et al, 2009. Another cadherin was found to be down-regulated and to exhibit genomic signature of selection in a Bti resistant Aedes aegypti strain, suggesting its implication in resistance, but there is not so far validation of its role as a receptor for Cry toxin (Bonin et al, 2009).…”

Section: The Role Of Membrane Receptors In Resistancementioning

confidence: 99%

Using the Bio-Insecticide Bacillus Thuringiensis Israelensis in Mosquito Control

Després¹,

Lagneau²,

Frutos³

2011

Pesticides in the Modern World - Pests Control and Pesticides Exposure and Toxicity Assessment

View full text Add to dashboard Cite

Proteomic identification of Bacillus thuringiensis subsp. israelensis toxin Cry4Ba binding proteins in midgut membranes from Aedes (Stegomyia) aegypti Linnaeus (Diptera, Culicidae) larvae

Cited by 75 publications

References 48 publications

Cadherin, Alkaline Phosphatase, and Aminopeptidase N as Receptors of Cry11Ba Toxin from Bacillus thuringiensis subsp. jegathesan in Aedes aegypti

Cadherin, Alkaline Phosphatase, and Aminopeptidase N as Receptors of Cry11Ba Toxin from Bacillus thuringiensis subsp. jegathesan in Aedes aegypti

Sodium Solute Symporter and Cadherin Proteins Act as Bacillus thuringiensis Cry3Ba Toxin Functional Receptors in Tribolium castaneum

Using the Bio-Insecticide Bacillus Thuringiensis Israelensis in Mosquito Control

Contact Info

Product

Resources

About