Literature DB >> 7592988

Identification, isolation, and cloning of a Bacillus thuringiensis CryIAc toxin-binding protein from the midgut of the lepidopteran insect Heliothis virescens.

S S Gill1, E A Cowles, V Francis.   

Abstract

Bacillus thuringiensis toxins are insecticidal to a variety of insect species. The selectivity of the toxins produced by these bacteria is dependent on both the toxin structure and the receptor sites that are present in different insect species. One of these toxins, CryIAc, is highly insecticidal to the noctuid pest Heliothis virescens. Using toxin overlay assay, a 120-kDa glycoprotein was identified as a toxin-binding protein. This protein was partially purified, its N-terminal sequence was determined, and the full-length cDNA encoding this protein was isolated from a H. virescens midgut library. The B. thuringiensis toxin-binding protein, BTBP1, has high homology to aminopeptidase N from eukaryotes and prokaryotes.

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Year:  1995        PMID: 7592988     DOI: 10.1074/jbc.270.45.27277

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  46 in total

1.  Characterization of a novel plasma membrane protein, expressed in the midgut epithelia of Bombyx mori, that binds to Cry1A toxins.

Authors:  Delwar M Hossain; Yasuyuki Shitomi; Kenta Moriyama; Masahiro Higuchi; Tohru Hayakawa; Toshiaki Mitsui; Ryoichi Sato; Hidetaka Hori
Journal:  Appl Environ Microbiol       Date:  2004-08       Impact factor: 4.792

2.  Formation of macromolecule complex with Bacillus thuringiensis Cry1A toxins and chlorophyllide binding 252-kDa lipocalin-like protein locating on Bombyx mori midgut membrane.

Authors:  Ganesh N Pandian; Toshiki Ishikawa; Thangavel Vaijayanthi; Delwar M Hossain; Shuhei Yamamoto; Tadayuki Nishiumi; Chanan Angsuthanasombat; Kohsuke Haginoya; Toshiaki Mitsui; Hidetaka Hori
Journal:  J Membr Biol       Date:  2010-11-16       Impact factor: 1.843

3.  Cadherin, alkaline phosphatase, and aminopeptidase N as receptors of Cry11Ba toxin from Bacillus thuringiensis subsp. jegathesan in Aedes aegypti.

Authors:  Supaporn Likitvivatanavong; Jianwu Chen; Alejandra Bravo; Mario Soberón; Sarjeet S Gill
Journal:  Appl Environ Microbiol       Date:  2010-10-29       Impact factor: 4.792

4.  Purification and characterization of Cry1Ac toxin binding proteins from the brush border membrane of Helicoverpa armigera midgut.

Authors:  Chunyan Liao; Stephen C Trowell; Ray Akhurst
Journal:  Curr Microbiol       Date:  2005-10-25       Impact factor: 2.188

Review 5.  Role of receptors in Bacillus thuringiensis crystal toxin activity.

Authors:  Craig R Pigott; David J Ellar
Journal:  Microbiol Mol Biol Rev       Date:  2007-06       Impact factor: 11.056

6.  A 104 kDa Aedes aegypti aminopeptidase N is a putative receptor for the Cry11Aa toxin from Bacillus thuringiensis subsp. israelensis.

Authors:  Jianwu Chen; Supaporn Likitvivatanavong; Karlygash G Aimanova; Sarjeet S Gill
Journal:  Insect Biochem Mol Biol       Date:  2013-10-12       Impact factor: 4.714

Review 7.  Phylogenetic relationships of Bacillus thuringiensis delta-endotoxin family proteins and their functional domains.

Authors:  A Bravo
Journal:  J Bacteriol       Date:  1997-05       Impact factor: 3.490

8.  Binding analyses of Bacillus thuringiensis Cry delta-endotoxins using brush border membrane vesicles of Ostrinia nubilalis.

Authors:  G Hua; L Masson; J L Jurat-Fuentes; G Schwab; M J Adang
Journal:  Appl Environ Microbiol       Date:  2001-02       Impact factor: 4.792

9.  Interaction of gene-cloned and insect cell-expressed aminopeptidase N of Spodoptera litura with insecticidal crystal protein Cry1C.

Authors:  Neema Agrawal; Pawan Malhotra; Raj K Bhatnagar
Journal:  Appl Environ Microbiol       Date:  2002-09       Impact factor: 4.792

10.  Binding of Bacillus thuringiensis Cry1Ac Toxin to Aminopeptidase in Susceptible and Resistant Diamondback Moths (Plutella xylostella).

Authors:  K Luo; B E Tabashnik; M J Adang
Journal:  Appl Environ Microbiol       Date:  1997-03       Impact factor: 4.792

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