کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1937223 | 1050711 | 2007 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: An ADAM metalloprotease is a Cry3Aa Bacillus thuringiensis toxin receptor An ADAM metalloprotease is a Cry3Aa Bacillus thuringiensis toxin receptor](/preview/png/1937223.png)
Bacillus thuringiensis insecticidal proteins toxic action relies on the interaction with receptor molecules on insect midgut target cells. Here, we describe an ADAM metalloprotease as a novel type of B. thuringiensis toxin receptor on the basis of the following data: (i) by ligand blot and N-terminal analysis, we detected a Colorado potato beetle Cry3Aa toxin binding molecule that shares homology with an ADAM10 metalloprotease; (ii) Colorado potato beetle brush border membrane vesicles display ADAM activity since it cleaves an ADAM fluorogenic substrate; (iii) Cry3Aa acts as a competitor of the cleavage of the ADAM fluorogenic substrate; (iv) Cry3Aa sequence contains the recognition motif R345FQPGYYGND354 present in ADAM10 substrates. Accordingly, a peptide representative of the recognition motif localized within loop 1 of Cry3Aa domain II (Ac-F341HTRFQPGYYGNDSFN358-NH2) effectively prevented Cry3Aa proteolytic processing and nearly abolished pore formation, evidencing the functional significance of the Cry3Aa–ADAM interaction in relation to this toxin mode of action.
Journal: Biochemical and Biophysical Research Communications - Volume 362, Issue 2, 19 October 2007, Pages 437–442