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Molecular Biotechnology

, Volume 60, Issue 8, pp 576–584 | Cite as

Effect of Temporal Expression of Integral Membrane Proteins by Baculovirus Expression Vector System

  • T. Z. Salem
  • F. Zhang
  • N. Sahly
  • S. Thiem
Original Paper

Abstract

Integral membrane proteins (IMPs) are popular target for drugs, but their resolved structures have been overlooked when compared with cytosolic proteins. The main reason is that IMPs usually need intensive post-translational modifications and they are bound to membranes, which increase the complexity of purifying or crystalizing them. Although different expression systems are used to express IMPs, baculovirus is considered one of the most successful expression systems for those proteins. Despite that, there are always unknown discrepancies in the level of IMPs expression in the baculovirus expression system. Retrospective studies have shown that expression of an immunoglobulin (anti-Chymase mouse monoclonal IgG1) driven by vp39 promoter was more efficient compared to its expression under polyhedrin (polh) promoter; however, this conclusion was not tested on different IMPs to generalize such a conclusion. In this study, the expression of eight different IMPs has been compared under vp39 and polh promoters of Autographa californica nucleopolyhedrovirus. Although different IMPs have shown different patterns of expression, the expression driven by vp39 promoter was found to be generally more efficient than the polh promoter.

Keywords

IMPs Vp39 promoter Polyhedrin promoter Baculovirus expression system Sf21 insect cells 

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Biomedical SciencesUniversity of Science and Technology at Zewail CityGizaEgypt
  2. 2.Department of Microbial GeneticsAGERI, Agricultural Research CenterGizaEgypt
  3. 3.Department of EntomologyMichigan State UniversityEast LansingUSA
  4. 4.Department of Microbiology and Molecular GeneticsMichigan State UniversityEast LansingUSA

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