Flexibility and strictness in functional replacement of domain III of cry insecticidal proteins from Bacillus thuringiensis

Hiroshi Sakai; Mohammad Tofazzal Hossain Howlader; Yumiko Ishida; Akiko Nakaguchi; Keiko Oka; Kouji Ohbayashi; Masashi Yamagiwa; Tohru Hayakawa

doi:10.1263/jbb.103.381

Flexibility and strictness in functional replacement of domain III of cry insecticidal proteins from Bacillus thuringiensis

Hiroshi Sakai, Mohammad Tofazzal Hossain Howlader, Yumiko Ishida, Akiko Nakaguchi, Keiko Oka, Kouji Ohbayashi, Masashi Yamagiwa, Tohru Hayakawa

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

Cry1C, one of the lepidopteran-specific insecticidal proteins from Bacillus thuringiensis, exhibits potent cytotoxicity against Sf9, an insect cell line. Cry1Aa and Cry4A, which are lepidopteran- and dipteran-specific insecticidal proteins, respectively, show no cytotoxicity against Sf9. When domain III of Cry1C was replaced with that of Cry1Aa or Cry4A, the hybrid Cry1C protein retained the cytotoxicity. These results suggest that domain III of Cry1C is not crucial in determining the cytocidal specificity of Cry1C against Sf9.

Original language	English
Pages (from-to)	381-383
Number of pages	3
Journal	Journal of Bioscience and Bioengineering
Volume	103
Issue number	4
DOIs	https://doi.org/10.1263/jbb.103.381
Publication status	Published - Apr 2007

Keywords

Bacillus thuringiensis
Cry protein
Sf9
cytotoxicity
domain exchange

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1263/jbb.103.381

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title = "Flexibility and strictness in functional replacement of domain III of cry insecticidal proteins from Bacillus thuringiensis",

abstract = "Cry1C, one of the lepidopteran-specific insecticidal proteins from Bacillus thuringiensis, exhibits potent cytotoxicity against Sf9, an insect cell line. Cry1Aa and Cry4A, which are lepidopteran- and dipteran-specific insecticidal proteins, respectively, show no cytotoxicity against Sf9. When domain III of Cry1C was replaced with that of Cry1Aa or Cry4A, the hybrid Cry1C protein retained the cytotoxicity. These results suggest that domain III of Cry1C is not crucial in determining the cytocidal specificity of Cry1C against Sf9.",

keywords = "Bacillus thuringiensis, Cry protein, Sf9, cytotoxicity, domain exchange",

author = "Hiroshi Sakai and Howlader, {Mohammad Tofazzal Hossain} and Yumiko Ishida and Akiko Nakaguchi and Keiko Oka and Kouji Ohbayashi and Masashi Yamagiwa and Tohru Hayakawa",

year = "2007",

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doi = "10.1263/jbb.103.381",

language = "English",

volume = "103",

pages = "381--383",

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T1 - Flexibility and strictness in functional replacement of domain III of cry insecticidal proteins from Bacillus thuringiensis

AU - Sakai, Hiroshi

AU - Howlader, Mohammad Tofazzal Hossain

AU - Ishida, Yumiko

AU - Nakaguchi, Akiko

AU - Oka, Keiko

AU - Ohbayashi, Kouji

AU - Yamagiwa, Masashi

AU - Hayakawa, Tohru

PY - 2007/4

Y1 - 2007/4

N2 - Cry1C, one of the lepidopteran-specific insecticidal proteins from Bacillus thuringiensis, exhibits potent cytotoxicity against Sf9, an insect cell line. Cry1Aa and Cry4A, which are lepidopteran- and dipteran-specific insecticidal proteins, respectively, show no cytotoxicity against Sf9. When domain III of Cry1C was replaced with that of Cry1Aa or Cry4A, the hybrid Cry1C protein retained the cytotoxicity. These results suggest that domain III of Cry1C is not crucial in determining the cytocidal specificity of Cry1C against Sf9.

AB - Cry1C, one of the lepidopteran-specific insecticidal proteins from Bacillus thuringiensis, exhibits potent cytotoxicity against Sf9, an insect cell line. Cry1Aa and Cry4A, which are lepidopteran- and dipteran-specific insecticidal proteins, respectively, show no cytotoxicity against Sf9. When domain III of Cry1C was replaced with that of Cry1Aa or Cry4A, the hybrid Cry1C protein retained the cytotoxicity. These results suggest that domain III of Cry1C is not crucial in determining the cytocidal specificity of Cry1C against Sf9.

KW - Bacillus thuringiensis

KW - Cry protein

KW - Sf9

KW - cytotoxicity

KW - domain exchange

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AN - SCOPUS:34248183544

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Flexibility and strictness in functional replacement of domain III of cry insecticidal proteins from Bacillus thuringiensis

Abstract

Keywords

ASJC Scopus subject areas

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