Abstract：
:Bacillus thuringiensis Cry toxins recognizes their target cells in part by the binding to glycosyl-phosphatidyl-inositol (GPI) anchored proteins such as aminopeptidase-N (APN) or alkaline phosphatases (ALP). Treatment of Tenebrio molitor brush border membrane vesicles (BBMV) with phospholipase C that cleaves out GPI-anchored proteins from the membranes, showed that GPI-anchored proteins are involved in binding of Cry3Aa toxin to BBMV. A 68 kDa GPI-anchored ALP was shown to bind Cry3Aa by toxin overlay assays. The 68 kDa GPI-anchored ALP was preferentially expressed in early instar larvae in comparison to late instar larvae. Our work shows for the first time that GPI-anchored ALP is important for Cry3Aa binding to T. molitor BBMV suggesting that the mode of action of Cry toxins is conserved in different insect orders.
journal_name
Peptidesjournal_title
Peptidesauthors
Zúñiga-Navarrete F,Gómez I,Peña G,Bravo A,Soberón Mdoi
10.1016/j.peptides.2012.05.019subject
Has Abstractpub_date
2013-03-01 00:00:00pages
81-6eissn
0196-9781issn
1873-5169pii
S0196-9781(12)00253-7journal_volume
41pub_type
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