Abstract
Sonchus yellow net virus (SYNV) proteins separate into four major and three minor proteins during polyacrylamide gel electrophoresis (PAGE). The major proteins consist of a glyoprotein (G), a nucleoprotein (N), and two proteins thought to be membrane proteins (M-1 and M-2). Minor proteins include two or three high molecular weight proteins (L) and a protein (possibly NS) with an electrophoretic mobility near the N protein. Proteins of potato yellow dwarf virus (PYDV) are similar in number and staining intensity to those of SYNV after PAGE, but the electrophoretic mobilities of proteins from the two viruses differ. SYNV dissociates with 2% Triton X-100 in 0.4 M NaCl at pH 7.5 to produce a 250 S nucleoprotein core plus solubilized L, G, and M proteins. A 200 S core is released at pH 7.5 in 0.8 M NaCl or at pH 8.4 in 0.4 or 0.8 M NaCl. The 250 S core contains all of the N protein and some undissociated L, G, and M proteins, but the 200 S core contains N protein and only traces of the L, G, and M proteins. After fixation with glutaraldehyde and negative staining, both 200 and 250 S cores are loosely coiled strands with a helical structure. The cores are infectious after being treated with detergent and separated on sucrose gradients, but the infectivity is considerably less than intact virus preparations. Iodination patterns of intact and detergent-disrupted virions suggest that L and G proteins are on the exterior of the virion, that M-2 is partially exposed on the virion surface, and that M-1 and N proteins are located beneath the surface of the virion.
Published Version
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