VESICULAR STOMATITIS VIRUS-MEDIATED CELL FUSION SUBSEQUENT TO VIRUS ADSORPTION AT DIFFRENT pH VALUES

Nagata, Satoshi; Kurata, Takeshi; Ueno, Yoshio; Chiba, Joe

doi:10.7883/yoken1952.44.171

Cited by 3 publications

(3 citation statements)

References 21 publications

(15 reference statements)

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“…It is possible that glycosylation at N336 plays a role in spike–spike interactions during fusion. This hypothesis fits well with the data presented here, and it would be interesting to study the potential correlation between endosomal pH of different cell types and their transduction by pseudotyped retroviruses containing variable amounts of VSV‐G, the importance of which has been alluded to in experiments showing that tightly regulated changes in pH are vital for the fusion reaction 71.…”

Section: Discussionsupporting

confidence: 86%

Factors that influence VSV‐G pseudotyping and transduction efficiency of lentiviral vectors—in vitro and in vivo implications

Farley

Iqball

Smith

et al. 2007

The Journal of Gene Medicine

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Pseudotyping viral vectors with vesicular stomatitis virus glycoprotein (VSV-G) enables the transduction of an extensive range of cell types from different species. We have discovered two important parameters of the VSV-G-pseudotyping phenomenon that relate directly to the transduction potential of lentiviral vectors: (1) the glycosylation status of VSV-G, and (2) the quantity of glycoprotein associated with virions. We measured production-cell and virion-associated quantities of two isoform variants of VSV-G, which differ in their glycosylation status, VSV-G1 and VSV-G2, and assessed the impact of this difference on the efficiency of mammalian cell transduction by lentiviral vectors. The glycosylation of VSV-G at N336 allowed greater maximal expression of VSV-G in HEK293T cells, thus facilitating vector pseudotyping. The transduction of primate cell lines was substantially affected (up to 50-fold) by the degree of VSV-G1 or VSV-G2 incorporation, whereas other cell lines, such as D17 (canine), were less sensitive to virion-associated VSV-G1/2 quantities. These data indicate that the minimum required concentration of virion-associated VSV-G differs substantially between cell species/types. The implications of these data with regard to VSV-G-pseudotyped vector production, titration, and use in host-cell restriction studies, are discussed.

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Section: Discussionsupporting

confidence: 86%

Factors that influence VSV‐G pseudotyping and transduction efficiency of lentiviral vectors—in vitro and in vivo implications

Farley

Iqball

Smith

et al. 2007

The Journal of Gene Medicine

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“…VSV-induced membrane fusion occurs at a very narrow pH range and can be avoided by different pH or other factors. [18][19][20] It is conceivable that the culture medium used during the transwell experiments allows release of already cellbound but not fused lentiviral particles. Whether this is a unique property of VSV-G pseudotyped viral particles or can also be observed when using other viral protein envelopes remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

Shuttle of lentiviral vectors via transplanted cells in vivo

et al. 2004

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“…The effect of MAbs on VSV-mediated cell fusion was assayed by inhibition of polykaryon formation of BHK-21 cells [24,38]. The cells in 24-well culture plates (about 1.5 x 105 celts/well) for 18-24 h were washed twice with the ice-cold binding medium (bicarbonatefree MEM buffered with 20 mM HEPES, pH 7.2, containing 2 mg/ml of BSA).…”

Section: Inhibition Of Vsv-mediated Cell Fusionmentioning

confidence: 99%

Identification of epitopes associated with different biological activities on the glycoprotein of vesicular stomatitis virus by use of monoclonal antibodies

Nagata

Okamoto

Inoue

et al. 1992

Archives of Virology

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Thirteen monoclonal antibodies (MAbs) to the glycoprotein (G) of vesicular stomatitis virus (VSV) serotype Indiana were prepared and examined for their effects on various biological activities of VSV, including in vitro infection, hemagglutination, adsorption to cells, and mediation of cell fusion. Competitive binding assays with these MAbs revealed the presence of at least seven distinct antigenic determinants (epitopes) on the G protein. In some cases, overlappings among epitopes to various degrees were observed as partial inhibition or binding enhancement. The MAbs to all the epitopes but one (epitopes 1-6) reacted with the denatured G protein in a Western immunoblot analysis. Four of the epitopes (epitopes 2, 4, 5, and 7) were involved in neutralization and two (epitopes 1 and 2) in hemagglutination inhibition. None of the MAbs inhibited the adsorption of radiolabeled VSV to BHK-21 cells; the MAbs to epitope 2 slightly enhanced the virus adsorption. All neutralization epitopes except epitope 2 (epitopes 4, 5, and 7) were associated with inhibition of VSV-mediated cell fusion. These results show a direct spatial relationship between the epitopes recognized by the MAbs and functional sites on G protein and further insights into the structure and function of G protein.

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VESICULAR STOMATITIS VIRUS-MEDIATED CELL FUSION SUBSEQUENT TO VIRUS ADSORPTION AT DIFFRENT pH VALUES

Cited by 3 publications

References 21 publications

Factors that influence VSV‐G pseudotyping and transduction efficiency of lentiviral vectors—in vitro and in vivo implications

Factors that influence VSV‐G pseudotyping and transduction efficiency of lentiviral vectors—in vitro and in vivo implications

Shuttle of lentiviral vectors via transplanted cells in vivo

Identification of epitopes associated with different biological activities on the glycoprotein of vesicular stomatitis virus by use of monoclonal antibodies

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