[1] Estruch J J, Warren G W, Mullins M A, Nye G J, Craig J A, Koziel M G. Vip3A, a novel Bacillus thuringiensis vegetative insecticidal protein with a wide spectrum of activities against Lepidopteran insects. Proceedings of the National Academy of Sciences of the United States of America, 1996, 93: 5389-5394.
[2] Lee M K, Walters F S, Hart H, Palekar N, Chen J S. The mode of action of the Bacillus thuringiensis vegetative insecticidal protein Vip3A differs from that of Cry1Ab δ-endotoxin. Applied and Environmental Microbiology, 2003, 69(8): 4648-4657.
[3] Donovan W P, Donovan J C, Engleman J T. Gene knockout demonstrates that vip3A contributes to the pathogenesis of Bacillus thuringiensis toward Agrotis ipsilon and Spodoptera exigua. Journal of Invertebrate Pathology, 2001, 78(1): 45-51.
[4] Yu C G, Mullins M A, Warren G W, Koziel M G, Estruch J J. The Bacillus thuringiensis vegetative insecticidal protein Vip3A lyses midgut epithelium cells of susceptible insects. Applied and Environmental Microbiology, 1997, 63(2): 532-536.
[5] Chakroun M, Ferré J. In vivo and in vitro binding of Vip3Aa to Spodoptera frugiperda midgut and characterization of binding sites by 125I radiolabeling. Applied and Environmental Microbiology, 2014, 80(20): 6258-6265.
[6] 张彦, 梁革梅, 张丽丽, 魏纪珍. 棉铃虫幼虫取食Vip3Aa蛋白后的中肠组织病理变化. 昆虫学报, 2012, 55(7): 869-876.
Zhang Y, Liang G M, Zhang L L, Wei J Z. Pathological changes in midgut tissues of larvae of the cotton bollworm, Helicoverpa armigera (Lepidoptera: Noctuidae), after feeding Vip3Aa protein. Acta Entomologica Sinica, 2012, 55(7): 869-876. (in Chinese)
[7] Liu J G, Yang A Z, Shen X H, Hua B G, Shi G L. Specific binding of activated Vip3Aa10 to Helicoverpa armigera brush border membrane vesicles results in pore formation. Journal of Invertebrate Pathology, 2011, 108(2): 92-97.
[8] Lee M K, Miles P, Chen J S. Brush border membrane binding properties of Bacillus thuringiensis Vip3A toxin to Heliothis virescens and Helicoverpa zea midguts. Biochemical and Biophysical Research Communications, 2006, 339(4): 1043-1047.
[9] Sena J A D, Hernández-Rodríguez C S, Ferré J. Interaction of Bacillus thuringiensis Cry1 and Vip3A proteins with Spodoptera frugiperda midgut binding sites. Applied and Environmental Microbiology, 2009, 75(7): 2236-2237.
[10] Caccia S, Chakroun M, Vinokurov K, Ferré J. Proteolytic processing of Bacillus thuringiensis Vip3A proteins by two Spodoptera species. Journal of Insect Physiology, 2014, 67: 76-84.
[11] Abdelkefi-Mesrati L, Boukedi H, Dammak-Karray M, Sellami- Boudawara T, Jaoua S, Tounsi S. Study of the Bacillus thuringiensis Vip3Aa16 histopathological effects and determination of its putative binding proteins in the midgut of Spodoptera littoralis. Journal of Invertebrate Pathology, 2010, 106(2): 250-254.
[12] Singh G, Sachdev B, Sharma N, Seth R, Bhatnagar R K. Interaction of Bacillus thuringiensis vegetative insecticidal protein with ribosomal S2 protein triggers larvicidal activity in Spodoptera frugiperda. Applied and Environmental Microbiology, 2010, 76(21): 7202-7209.
[13] Smith G P. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science, 1985, 228: 1315-1317.
[14] 丁宁, 肖慧, 高巨, 许立新, 佘守章. 应用噬菌体展示技术筛选HMGB启动子结合蛋白. 中国病理生理杂志, 2010, 26(1): 28-31.
Ding N, Xiao H, Gao J, Xu L X, She S Z. Screening of binding proteins of HMGB1 promoter by phage display technique. Chinese Journal of Pathophysiology, 2010, 26(1): 28-31. (in Chinese)
[15] Fernández L E, Gómez I, Pacheco S, Arenas I, Gilla S S, Bravo A, Soberón M. Employing phage display to study the mode of action of Bacillus thuringiensis Cry toxins. Peptides, 2008, 29(2): 324-329.
[16] Gómez I, Oltean D, Gill S S, Bravo A, Soberón M. Mapping the epitope in cadherin-like receptors involved in Bacillus thuringiensis Cry1A toxin interaction using phage display. The Journal of Biological Chemistry, 2001, 276(31): 28906-28912.
[17] Guo C H, Zhao S T, Ma Y, Hu J J, Han X J, Chen J, Lu M Z. Bacillus thuringiensis Cry3Aa fused to a cellulase-binding peptide shows increased toxicity against the longhorned beetle. Applied Microbiology and Biotechnology, 2012, 93(3): 1249-1256.
[18] Wang Y, Zhang X, Zhang C, Liu Y, Liu X. Isolation of single chain variable fragment (scFv) specific for Cry1C toxin from human single fold scFv libraries. Toxicon, 2012, 60(7): 1290-1297.
[19] Wolfersberger M, Luethy P, Maurer A, Parenti P, Sacchi F V, Giordana B, Hanozet G M. Preparation and partial characterization of amino acid transporting brush border membrane vesicles from the larval midgut of the cabbage butterfly (Pieris brassicae). Comparative Biochemistry and Physiology A, 1987, 86(2): 301-308.
[20] Silva-Filha M H, Nielsen-LeRoux C, Charles J F. Identification of the receptor for Bacillus sphaericus crystal toxin in the brush border membrane of the mosquito Culex pipiens (Diptera: Culicidae). Insect Biochemistry and Molecular Biology, 1999, 29: 711-721.
[21] Pigott C R, Ellar D J. Role of receptors in Bacillus thuringiensis crystal toxin activity. Microbiology and Molecular Biology Reviews, 2007, 71(2): 255-281.
[22] Pardo-López L, Soberón M, Bravo A. Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection. FEMS Microbiology Reviews, 2013, 37(1): 3-22.
[23] Palma L, Muñoz D, Berry C, Murillo J, Caballero P. Bacillus thuringiensis toxins: an overview of their biocidal activity. Toxins, 2014, 6(12): 3296-3325. |