کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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20586 | 43181 | 2012 | 6 صفحه PDF | دانلود رایگان |
The human (pro)renin receptor (hPRR) was displayed on the surface of Bombyx mori nucleopolyhedrovirus (BmNPV) with and without fusion to glycoprotein 64 (GP64) of the BmNPV. hPRR1 is a native hPRR with an additional FLAG peptide sequence inserted between the signal peptide and prorenin-binding domain. hPRR2 has the prorenin-binding domain inserted between amino acid residues 81Asp and 82Pro of GP64. hPRR4 has the prorenin-binding domain inserted in 81Asp and 320Met of partially deleted GP64. Incorporation of hPRR was confirmed in recombinant BmNPV (rBmNPV) but not in cysteine protease-deleted rBmNPV. hPRR1 was observed in ER, but hPRR2 and hPRR4 were observed around the endoplasmic reticulum (ER) and in its periphery. rBmNPV-hPRR1 and -hPRR2, carrying hPRR1 and hPRR2 respectively, showed binding affinity to human renin, but rBmNPV-hPRR4 did not. The presence of hPRR4 of rBmNPV-hPRR4 was confirmed in western blotting under nonreducing conditions, suggesting that although hPRR4 was incorporated in rBmNPV-hPRR4, it behaved as a non-functional aggregate. This rBmNPV display system can also be used for analyzing a ligand–receptor interaction.
Journal: Journal of Bioscience and Bioengineering - Volume 114, Issue 5, November 2012, Pages 564–569