کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4558528 | 1329946 | 2008 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Disruption of Ha_BtR alters binding of Bacillus thuringiensis δ-endotoxin Cry1Ac to midgut BBMVs of Helicoverpa armigera
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
بوم شناسی، تکامل، رفتار و سامانه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Disruption of Ha_BtR alters binding of Bacillus thuringiensis δ-endotoxin Cry1Ac to midgut BBMVs of Helicoverpa armigera Disruption of Ha_BtR alters binding of Bacillus thuringiensis δ-endotoxin Cry1Ac to midgut BBMVs of Helicoverpa armigera](/preview/png/4558528.png)
چکیده انگلیسی
Disruption of the Ha_BtR (a cadherin gene) is genetically linked to resistance to Cry1Ac δ-endotoxin of Bacillus thuringiensis in the GYBT strain of Helicoverpa armigera. Brush border membrane vesicles (BBMVs) prepared from midguts of both the Cry1Ac-resistant GYBT strain (homozygous for a deletion knockout of Ha_BtR) and the susceptible GY strain (homozygous for the wild type of Ha_BtR) possessed saturable and specific binding ability to 125I-Cry1Ac. The binding constant (Kd) of the GY strain was significantly lower than that of the resistant GYBT strain, whereas their binding site concentrations (Bmax) were similar. When midgut BBMVs were reacted directly with streptavidin conjugated to horseradish peroxidase, the GY strain had very clear 120- and 85-kDa protein bands, which indicated that the 120- and 85-kDa bands are endogenous biotin-containing proteins. However, the GYBT strain almost completely lost these two biotin-containing proteins. Ligand blotting with biotinylated Cry1Ac toxin showed midgut BBMVs of the GY strain contain five protein bands of 210-, 190-, 150-, 120-, and 85-kDa, respectively, while BBMVs of the GYBT strain contain only two protein bands of 150- and 120-kDa. 120-kDa bands may consist of two proteins with coincidentally the same molecular weight (putatively, an APN and a biotin-containing protein). Our results showed that the binding pattern of Cry1Ac to midgut BBMVs of H. armigera was altered quantitatively and qualitatively by knockout of Ha_BtR. There are multiple Cry1Ac-binding proteins in the midgut of susceptible H. armigera, but only the Ha_BtR can be considered as a putative functional receptor of Cry1Ac. Possible involvement of other receptor proteins in the intoxication process in vivo could not be excluded.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Invertebrate Pathology - Volume 97, Issue 1, January 2008, Pages 27-32
Journal: Journal of Invertebrate Pathology - Volume 97, Issue 1, January 2008, Pages 27-32
نویسندگان
Xinjun Xu, Yidong Wu,