کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2021007 | 1542351 | 2010 | 7 صفحه PDF | دانلود رایگان |
The pentameric B subunit of cholera toxin (CtxB) is an efficient mucosal adjuvant for vaccines. We report the expression of a chimeric protein comprising the synthetic cholera toxin B subunit fused at its C-terminal with rabies surface glycoprotein (G protein) in tobacco plants. The ∼80.3 kDa fusion polypeptide expressed at 0.4% of the total soluble protein in leaves of the selected transgenic lines. The fusion protein formed a ∼403 kDa pentameric protein which was functionally active in binding to GM1 receptor. The plant-made protein had a higher affinity for GM1 receptor than the native bacterial CtxB. The pentameric fusion protein was recognized by the anti-cholera toxin as well as anti-rabies antibodies. Its immuno-protective ability against rabies remains to be examined.
Journal: Protein Expression and Purification - Volume 70, Issue 2, April 2010, Pages 184–190