Skip to main content
. 2003 Jun;77(11):6438–6449. doi: 10.1128/JVI.77.11.6438-6449.2003

FIG. 8.

FIG. 8.

Characterization of effect of VP1 coexpression on VP3 proteolytic processing and subcellular distribution of capsid proteins. (A) Detection of VP1 and VP3 polypeptides that accumulated in FB/Poly- and FBD/Poly-VP1-infected cells. Infected cells were harvested at 24, 48, 72, and 96 h postinfection. The samples were analyzed by Western blot with anti-VP1 and -VP3 sera, followed by addition of horseradish peroxidase-conjugated goat anti-rat immunoglobulin. The signal was detected by enhanced chemiluminescence. The position of molecular mass markers (in kilodaltons) are indicated. (B) The subcellular distribution of pVP2/VP2 and VP3 polypeptides in cells infected with FB/Poly and FBD/Poly-VP1 was analyzed by confocal laser scanning microscopy. At 60 h postinfection, cells were fixed and incubated with rabbit anti-pVP2/VP2 and rat anti-VP3, followed by incubation with goat anti-rabbit immunoglobulin coupled to Alexa 488 (green) and goat anti-rat immunoglobulin coupled to Alexa 594 (red). Arrowheads indicate the positions of viroplasm-like areas containing pVP2/VP2 and VP3.