[논문]Stability of Retroviral Vectors Against Ultracentrifugation Is Determined by the Viral Internal Core and Envelope Proteins Used for Pseudotyping

Kim, Soo-hyun; Lim, Kwang-il

doi:10.14348/molcells.2017.0043

Stability of Retroviral Vectors Against Ultracentrifugation Is Determined by the Viral Internal Core and Envelope Proteins Used for Pseudotyping 원문보기

Molecules and cells, v.40 no.5, 2017년, pp.339 - 345

Kim, Soo-hyun (Department of Chemical and Biological Engineering, Sookmyung Women's University) , Lim, Kwang-il (Department of Chemical and Biological Engineering, Sookmyung Women's University)

Abstract ▼ AI-Helper

Retroviral and lentiviral vectors are mostly pseudotyped and often purified and concentrated via ultracentrifugation. In this study, we quantified and compared the stabilities of retroviral [murine leukemia virus (MLV)-based] and lentiviral [human immunodeficiency virus (HIV)-1-based] vectors pseudotyped with relatively mechanically stable envelope proteins, vesicular stomatitis virus glycoproteins (VSVGs), and the influenza virus WSN strain envelope proteins against ultracentrifugation. Lentiviral genomic and functional particles were more stable than the corresponding retroviral particles against ultracentrifugation when pseudotyped with VSVGs. However, both retroviral and lentiviral particles were unstable when pseudotyped with the influenza virus WSN strain envelope proteins. Therefore, the stabilities of pseudotyped retroviral and lentiviral vectors against ultracentrifugation process are a function of not only the type of envelope proteins, but also the type of viral internal core (MLV or HIV-1 core). In addition, the fraction of functional viral particles among genomic viral particles greatly varied at times during packaging, depending on the type of envelope proteins used for pseudotyping and the viral internal core.

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However, the complete understanding of how stabilities of retroviral vectors are determined is still elusive. In this study, we found that the stability of pseudotyped viruses against ultracentrifugation is a function of not only the mechanical stability of envelope proteins, but also the type of viral internal core. Additionally, the conventionally obtainable degree to which pseudotyped viral particles are concentrated by ultracentrifugation, i.

제안 방법

In this study, we quantified the stabilities of retroviral and lentiviral vectors pseudotyped with influenza virus envelope proteins, hemagglutinin (HA) and neuraminidase (NA), against ultracentrifugation. Retroviral and lentiviral vectors with the influenza virus surface proteins can be used in studies to advance influenza virus vaccines (Tao et al.

성능/효과

5 h spin at 25,000 rpm). After this second round of ultracentrifugation, 58.9% of the remaining gMLV-VSVG particles and 20.6% of the remaining tMLV-VSVG particles were further lost (Fig. 3). Therefore, a significant fraction of viral particles in the samples can be lost during ultracentrifugation even after being pseudotyped with relatively mechanically stable envelope proteins.
However, this advantage of using the HIV-1 core rather than the MLV core to achieve higher stability of functional viral particles, as observed for pseudotyping with VSVGs, did not apply to pseudotyping with the WSN surface proteins. First, 26.4% and 67.3% of HIV1-WSN genomic particles (gHIV1-WSN) in the first and second harvests survived the first round of ultracentrifugation (73.6% and 32.7% losses, respectively) (Fig. 6A). These stabilities were higher than those observed for gMLV-WSN particles (Figs.
5B). From this result it was noted that MLV transducing vector particles became even less stable when pseudotyped with the influenza virus WSN strain envelope proteins than when pseudotyped with VSVGs.

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Stability of Retroviral Vectors Against Ultracentrifugation Is Determined by the Viral Internal Core and Envelope Proteins Used for Pseudotyping 원문보기

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Stability of Retroviral Vectors Against Ultracentrifugation Is Determined by the Viral Internal Core and Envelope Proteins Used for Pseudotyping 원문보기

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