Phage display of Bacillus thuringiensis CryIA(a) insecticidal toxin

FEBS Letters

Selvapandiyan, Angamuthu³  Bradbury, Andrew²  Edomi, Paolo¹  Bhatnagar, Raj K³  Ahmad, Suhail³  Marzari, Roberto¹ 

[1] Dipartimento di Biologia, Universita' degli Studi di Trieste, via E. Weiss 2, 34127 Trieste, Italy;International School for Advanced Studies (SISSA), via Beirut 2/4, 34012 Trieste, Italy;International Centre for Genetic Engineering and Biotechnology, ICGEB Campus, Aruna Asaf Ali Marg, 110067 New Delhi, India

关键词: Phage display;    Phagemid;    δ-Endotoxin;    Insecticidal crystal protein;   

DOI  :  10.1016/S0014-5793(97)00647-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The display of proteins or peptides on the surface of filamentous phages or phagemids has been shown to be a very powerful technology for the rescue of specific binders from large combinatorial libraries, as well as to select derivatives of known proteins with altered binding properties. The Bacillus thuringiensis (Bt) crystal proteins are a large family of insecticidal toxins which bind to receptors found on the brush border of larval midgut cells, different crystal toxins having different larval specificities. Here we describe the display of different CryIA(a) toxin regions on the surface of phagemids using the display vector pHEN1, the purpose being the identification of toxin sequences suitable for mutagenesis and selection using phage display. We show that CryIA(a) domain II, in which the receptor binding activity is located, is efficiently displayed as well as being secreted as soluble protein into the periplasm of bacterial cell. This forms the basis of a simple means for the modification of toxin specificity and the selection of toxin proteins with novel or expanded host ranges.

【 授权许可】

Unknown