Signaling versus punching hole: How do Bacillus thuringiensis toxins kill insect midgut cells?

被引：184

作者：

Soberon, M. ^{[1
]}

Gill, S. S. ^{[2
]}

Bravo, A. ^{[1
]}

机构：

[1] Univ Nacl Autonoma Mexico, Inst Biotecnol, Cuernavaca 62250, Morelos, Mexico

[2] Univ Calif Riverside, Dept Cell Biol & Neurosci, Riverside, CA 92506 USA

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2009年 / 66卷 / 08期

关键词：

Cry toxins; Bacillus thuringiensis; pore formation; signal transduction; toxin receptors; oligomerization; Cry toxin resistance; MANDUCA-SEXTA MIDGUT; BRUSH-BORDER MEMBRANES; AMINOPEPTIDASE-N; DELTA-ENDOTOXIN; HELIOTHIS-VIRESCENS; CRY1AB TOXIN; PORE FORMATION; CADHERIN-LIKE; BOMBYX-MORI; DOMAIN-III;

D O I：

10.1007/s00018-008-8330-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cry proteins, produced by Bacillus thuringiensis (Bt), are widely used for the control of insect pests in agriculture as spray products or expressed in transgenic crops, such as maize and cotton. Little was known regarding the mechanism of action of these toxins when the first commercial Bt product was introduced fifty years ago. However, research on the mechanism of action over the last two decades has enhanced our knowledge of toxin interaction with membrane receptors and their effects in insect midgut cells. All this information allowed for the rational design of improved toxins with higher toxicity or toxins that overcome insect resistance, which could compromise Bt use and effectiveness in the field. In this review we discuss and evaluate the different models of the mode of action of Cry toxins, including a discussion about the role of various receptors in toxin action.

引用

页码：1337 / 1349

页数：13

共 103 条

[1]

Abdullah Mohd Amir F., 2006, BMC Biochemistry, V7, DOI 10.1186/1471-2091-7-16

[2] Interaction of gene-cloned and insect cell-expressed aminopeptidase N of Spodoptera litura with insecticidal crystal protein Cry1C [J].

Agrawal, N ;

Malhotra, P ;

Bhatnagar, RK .

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2002, 68 (09) :4583-4592

[3]

Aronson AI, 1999, APPL ENVIRON MICROB, V65, P2503

[4] Cloning of a Heliothis virescens 110 kDa aminopeptidase N and expression in Drosophila S2 cells [J].

Banks, DJ ;

Hua, G ;

Adang, M .

INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2003, 33 (05) :499-508

[5]

Becker N., 2000, Entomopathogenic Bacteria, P383, DOI DOI 10.1007/978-94-017-1429-7_21

[6] Structure of the functional form of the mosquito larvicidal Cry4Aa toxin from Bacillus thuringiensis at a 2.8-Angstrom resolution [J].

Boonserm, P ;

Mo, M ;

Angsuthanasombat, C ;

Lescar, J .

JOURNAL OF BACTERIOLOGY, 2006, 188 (09) :3391-3401

[7] Crystal structure of the mosquito-iarvicidal toxin Cry4Ba and its biological implications [J].

Boonserm, P ;

Davis, P ;

Ellar, DJ ;

Li, J .

JOURNAL OF MOLECULAR BIOLOGY, 2005, 348 (02) :363-382

[8] Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains [J].

Bravo, A ;

Gómez, I ;

Conde, J ;

Muñoz-Garay, C ;

Sánchez, J ;

Miranda, R ;

Zhuang, M ;

Gill, SS ;

Soberón, M .

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2004, 1667 (01) :38-46

[9] Coiled coils: a highly versatile protein folding motif [J].

Burkhard, P ;

Stetefeld, J ;

Strelkov, SV .

TRENDS IN CELL BIOLOGY, 2001, 11 (02) :82-88

[10] N-acetylgalactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin [J].

Burton, SL ;

Ellar, DJ ;

Li, J ;

Derbyshire, DJ .

JOURNAL OF MOLECULAR BIOLOGY, 1999, 287 (05) :1011-1022

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