2017
DOI: 10.1016/j.ibmb.2017.05.004
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Intra- and extracellular domains of the Helicoverpa armigera cadherin mediate Cry1Ac cytotoxicity

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Cited by 22 publications
(31 citation statements)
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“…The red line shows the putative toxin‐binding region of HaCad. No mutations were found in SCD or LF256 in amino acids 1,422–1,440, which are especially important in binding (Zhang et al., )…”
Section: Resultsmentioning
confidence: 99%
“…The red line shows the putative toxin‐binding region of HaCad. No mutations were found in SCD or LF256 in amino acids 1,422–1,440, which are especially important in binding (Zhang et al., )…”
Section: Resultsmentioning
confidence: 99%
“… Sequence Helicoverpa armigera (LOC 110371604) is a predicted cadherin-related tumor suppressor; sequence Helicoverpa armigera (BtR) (AY647974) is annotated as in [ 121 ], and additional information [ 127 , 128 ]; sequence Manduca sexta (BT-R1) (AF319973) is annotated as in [ 122 ]. EC = cadherin repeats (in red); TBR = putative Cry1Ac toxin binding region (in blue).…”
Section: Supporting Informationmentioning
confidence: 99%
“…Binding of a Cry toxin to the toxin binding region (TBR) on a cadherin receptor is required for further toxin cleavage, oligomerization and eventual pore-forming that is critical for intoxication [18]. Presently a number of cadherin mutations have been identified and some confer resistance to the Cry toxins in Heliothis virescens, Pectinophora gossypiella and Helicoverpa armigera [6,19,20]. Moreover, homozygous knockout of the cadherin gene in H. armigera confers resistance to the Cry1Ac toxin [21].…”
Section: Introductionmentioning
confidence: 99%