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. 2010 Feb 17;84(9):4737–4746. doi: 10.1128/JVI.02670-09

FIG. 5.

FIG. 5.

Calcium-site-mutated VLPs bind to DL-1 cells but cannot rescue the infectivity of maturation-defective FHV. (A) Progeny virus produced by coinfecting 1 × 108 Drosophila DL-1 cells with 1.5 × 103 particles/cell of D75N/N363T FHV and 9 × 103 particles/cell of wild-type VLPs or each of the mutated VLPs. [35S]methionine-cysteine-labeled progeny virus was quantified, with the amount of progeny produced during coinfection with D75N/N363T FHV and wild-type VLPs normalized at 100%. (B) FACS analysis of the binding of wild-type or mutated VLPs to 1 × 106 Drosophila DL-1 cells for 1 h at 4°C. Bound particles were detected using a rabbit polyclonal primary antibody against FHV capsid protein and a goat anti-rabbit secondary antibody conjugated with Alexa 488 (Molecular Probes). Five percent BSA was added to cells as a negative control, followed by antibody incubations. Data shown are representative of two separate experiments.