A 50-Kilodalton Cry2A Peptide Is Lethal to Bombyx mori and Lymantria dispar

Ohsawa, Masataka; Tanaka, Miki; Moriyama, Koichi; Shimazu, Mitsuaki; Asano, Sumitada; Miyamoto, Kazuhisa; Haginoya, Kohsuke; Mitsui, Toshiaki; Kouya, Tomoaki; Taniguchi, Masayuki; Hori, Hidetaka

doi:10.1128/aem.07123-11

Cited by 10 publications

(18 citation statements)

References 19 publications

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“…Previously, cleavage of the Cry2Aa1 and Cry2Aa3 protoxins by Lymantria dispar and B. mori larvae midgut juice produced two major bands, 58 and 49 kDa toxins. N-terminal sequencing confirmed that the first cleavage site was at Tyr49, which is on the loop between α-0 and α-1, while the second cleavage site was at Leu144, which is on the loop between α-3 and α-4 [35,36].…”

Section: Discussionmentioning

confidence: 92%

Proteolysis activation of Cry1Ac and Cry2Ab protoxins by larval midgut juice proteases from Helicoverpa armigera

Liu

Wang

et al. 2020

PLoS ONE

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Proteolytic processing of Bacillus thuringiensis (Bt) Cry protoxins by insect midgut proteases is critical to their insecticidal activities against target insects. Although transgenic Bt cotton expressing Cry1Ac and Cry2Ab proteins have been widely used for control of the cotton bollworm (Helicoverpa armigera) in the field, the proteolytic cleavage sites in the two protoxins targeted by H. armigera midgut proteases are still not clear. In this study, the proteolysis of Cry1Ac and Cry2Ab protoxins by midgut juice prepared from midgut tissue of H. armigera larvae was investigated. Cleavage of Cry1Ac protoxin by midgut proteases formed a major protein fragment of~65 kDa, and N-terminal sequencing revealed that cleavage occurred at Arg28 in the fore-end of helix α-1 in domain I of Cry1Ac. Cleavage of Cry2Ab protoxin by midgut juice proteases produced a major protein fragment of~50 kDa, and the cleavage occurred at Arg139 between helices α-3 and α-4 in domain I of Cry2Ab. The amino acids Arg28 of Cry1Ac and Arg139 of Cry2Ab were predicted as putative trypsin cleavage sites. Bioassay data showed that the toxicities (LC 50 s) of Cry1Ac and Cry2Ab protoxins were equivalent to those of their respective midgut juice-activated toxins in the susceptible SCD strain of H. armigera. Identification of the exact sites of N-terminal activation of Cry1Ac and Cry2Ab protoxins will provide a basis for a better understanding of the mode of action and resistance mechanisms based on aberrant activation of these protoxins in H. armigera.

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Section: Discussionmentioning

confidence: 92%

Proteolysis activation of Cry1Ac and Cry2Ab protoxins by larval midgut juice proteases from Helicoverpa armigera

Liu

Wang

et al. 2020

PLoS ONE

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“…The polymerase chain reaction (PCR) technique has been widely used for the identification and characterisation of Bt genes, including cry2A ‐type genes . In the present study, the PCR assay was used to identify the Cry content of the Bt strains under investigation using the set (Cry2A, Cry2B) amplifying a region of 570 bp.…”

Section: Resultsmentioning

confidence: 99%

“…The polymerase chain reaction (PCR) technique has been widely used for the identification and characterisation of Bt genes, including cry2A-type genes. 11,16,28,29 In the present study, the PCR assay was used to identify the Cry content of the Bt strains under investigation using the set (Cry2A, Cry2B) amplifying a region of 570 bp. The results revealed that only six (BUPM109, BLB30, BLB140, BLB200, BLB240 and MEB4) of the 15 selected strains could harbour the cry2A-type genes.…”

Section: Identification Of Cry2a-type Genesmentioning

confidence: 99%

“…However, the three‐dimensional structures of these two proteins are very similar . This structure similarity suggests that the mechanism by which Cry2Aa kills is highly similar to that of the other Cry toxins . The Cry2Aa protein is active against both lepidopteran and dipteran insects, whereas Cry2Ab, Cry2Ac and Cry2Ad are insecticidal only to lepidopteran insects .…”

Section: Introductionmentioning

confidence: 97%

“…9,10 This structure similarity suggests that the mechanism by which Cry2Aa kills is highly similar to that of the other Cry toxins. 11 The Cry2Aa protein is active against both lepidopteran and dipteran insects, whereas Cry2Ab, Cry2Ac and Cry2Ad are insecticidal only to lepidopteran insects. 12 The literature indicates that some of the latter proteins have also shown mild activity against mosquito larvae.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Molecular characterisation of Bacillus thuringiensis strain MEB4 highly toxic to the Mediterranean flour moth Ephestia kuehniella Zeller (Lepidoptera: Pyralidae)

Abdelmalek

Sellami

Kridis

et al. 2015

Pest Management Science

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CRISPR/Cas9 mediated genome editing of Helicoverpa armigera with mutations of an ABC transporter gene HaABCA2 confers resistance to Bacillus thuringiensis Cry2A toxins

Wang

Liu

et al. 2017

Insect Biochemistry and Molecular Biology

102

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A 50-Kilodalton Cry2A Peptide Is Lethal to Bombyx mori and Lymantria dispar

Abstract: ABSTRACTThe Cry2Aa3 gene was introduced into asporogenicBacillus thuringiensis, and the synthesized protoxin killedBombyx moriandLymantria disparlarvae. Chymotrypsin hydrolyzed the linkages between 49Tyr/Val50 and 145Lys/Ser146 in the protoxin, and 50- and 58-kDa fragment… Show more

Cited by 10 publications

References 19 publications

Proteolysis activation of Cry1Ac and Cry2Ab protoxins by larval midgut juice proteases from Helicoverpa armigera

Proteolysis activation of Cry1Ac and Cry2Ab protoxins by larval midgut juice proteases from Helicoverpa armigera

Molecular characterisation of Bacillus thuringiensis strain MEB4 highly toxic to the Mediterranean flour moth Ephestia kuehniella Zeller (Lepidoptera: Pyralidae)

CRISPR/Cas9 mediated genome editing of Helicoverpa armigera with mutations of an ABC transporter gene HaABCA2 confers resistance to Bacillus thuringiensis Cry2A toxins

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