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J Biosci Bioeng. 2012 Nov;114(5):564-9. doi: 10.1016/j.jbiosc.2012.06.008. Epub 2012 Jul 3.

Display of the human (pro)renin receptor on Bombyx mori nucleopolyhedrovirus (BmNPV) particles using Bm cells.

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  • 1Laboratory of Biotechnology, Faculty of Agriculture, Shizuoka University, 836 Ohya, Suruga-ku, Shizuoka 422-8529, Japan.

Abstract

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 (81)Asp and (82)Pro of GP64. hPRR4 has the prorenin-binding domain inserted in (81)Asp and (320)Met 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.

Copyright © 2012 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.

PMID:
22762973
[PubMed - indexed for MEDLINE]
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