Author: van der Schaar, H. M.; Melia, C. E.; van Bruggen, J. A. C.; Strating, J. R. P. M.; van Geenen, M. E. D.; Koster, A. J.; Bárcena, M.; van Kuppeveld, F. J. M.
Title: Illuminating the Sites of Enterovirus Replication in Living Cells by Using a Split-GFP-Tagged Viral Protein Document date: 2016_7_6
ID: 1aptufp6_29
Snippet: Next, we tested whether BGM cells became GFP fluorescent upon infection with CVB3-GFP(S1-10)-3A(S11aa2). Figure 7C shows that GFP fluorescence colocalized with 3A, visualized by using an anti-3A antibody, both early and later in infection. Yet, the GFP fluorescence was substantially dimmer compared to BGM(GFPS1-10) cells infected with CVB3-3A(S11aa2). It is plausible that the dimmer signal is a result of the equimolar ratios of 3A(S11aa2) and GFP.....
Document: Next, we tested whether BGM cells became GFP fluorescent upon infection with CVB3-GFP(S1-10)-3A(S11aa2). Figure 7C shows that GFP fluorescence colocalized with 3A, visualized by using an anti-3A antibody, both early and later in infection. Yet, the GFP fluorescence was substantially dimmer compared to BGM(GFPS1-10) cells infected with CVB3-3A(S11aa2). It is plausible that the dimmer signal is a result of the equimolar ratios of 3A(S11aa2) and GFP(S1-10) generated by this virus, while BGM(GFPS1-10) cells produce an excess of GFP(S1-10). Another explanation for the dim GFP fluorescence is the suboptimal cleavage of the artificial cleavage site. When GFP(S1-10) is still fused to P1, it might be unable to assemble with 3A(S11aa2) and/or become fluorescent. Nevertheless, these findings suggest that the virus containing both GFP fragments is suitable for live-cell imaging.
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