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Production of Vesicular Stomatitis Virus Glycoprotein-Pseudotyped Lentiviral Vector Is Enhanced by Ezrin Silencing. | LitMetric

Production of Vesicular Stomatitis Virus Glycoprotein-Pseudotyped Lentiviral Vector Is Enhanced by Ezrin Silencing.

Front Bioeng Biotechnol

Department of Molecular Microbiology and Immunology, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Japan.

Published: April 2020

AI Article Synopsis

  • HIV-1-based viral vectors are commonly used in gene therapy and can effectively introduce genes into target cells, especially when paired with VSV-G, which significantly enhances transduction efficiency.
  • This study reveals that the HIV-1 Gag protein is broken down in the lysosomes of COS7 cells, but the presence of VSV-G helps prevent this degradation, suggesting a protective mechanism.
  • The research highlights the role of unphosphorylated ezrin in reducing Gag protein levels and indicates that silencing ezrin can increase the yield of VSV-G-pseudotyped HIV-1 vectors, suggesting potential avenues for improving vector production.

Article Abstract

Human immunodeficiency virus type 1 (HIV-1)-based viral vector is widely used as a biomaterial to transfer a gene of interest into target cells in many biological study fields including gene therapy. Vesicular stomatitis virus glycoprotein (VSV-G)-containing HIV-1 vector much more efficiently transduces various mammalian cells than other viral envelope proteins-containing vectors. Understanding the mechanism would contribute to development of a novel method of efficient HIV-1 vector production. HIV-1 vector is generally constructed by transient transfection of human 293T or African green monkey COS7 cells. It was found in this study that HIV-1 Gag protein is constitutively digested in lysosomes of African green monkey cells. Surprisingly, VSV-G elevated HIV-1 Gag protein levels, suggesting that VSV-G protects Gag protein from the lysosomal degradation. Unphosphorylated ezrin, but not phosphorylated ezrin, was detected in COS7 cells, and ezrin silencing elevated Gag protein levels in the presence of VSV-G. Expression of unphosphorylated ezrin reduced Gag protein amounts. These results indicate that unphosphorylated ezrin proteins inhibit the VSV-G-mediated stabilization of HIV-1 Gag protein. Trafficking of HIV-1 Gag-associated intracellular vesicles may be controlled by ezrin. Finally, this study found that ezrin silencing yields higher amount of VSV-G-pseudotyped HIV-1 vector.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7201057PMC
http://dx.doi.org/10.3389/fbioe.2020.00368DOI Listing

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