Dimethyl Sulphoxide (DMSO) Disassembles Tobacco Mosaic Virus Predominantly from the 5'-end of the Viral RNA

Abstract

SUMMARYThe effect of dimethyl sulphoxide (DMSO) on the stability of native and EDTA-treated tobacco mosaic virus (TMV, Vulgare strain) has been reinvestigated using a variety of chemical and biochemical techniques. Contrary to earlier reports, we conclude that TMV rods behave as a heterodisperse population, exhibiting one of two modes of uncoating. More than 50% of the rods disassemble rapidly and extensively in a unique polar fashion beginning at the 5'-end of the viral RNA. The remainder of the rod population uncoats more slowly, less extensively, and exhibits substantial bidirectional exposure of the viral RNA, commencing at the 3'-terminus but proceeding for no more than 500 nucleotides before the major uncoating event again shifts to the 5'-ends of the particles. A portion of the coat protein gene and the region around the assembly initiation site on the viral RNA appears most resistant to uni-or bidirectional stripping; this is in contrast to previous reports. This complex, biphasic behaviour of the TMV rod population, which produces two broad and relatively ill-defined peaks of metastable nucleoprotein intermediates, may account for many of the inconsistencies prevalent in earlier work.

Nanoscale device architectures derived from biological assemblies: The case of tobacco mosaic virus and (apo)ferritin

“…56) It infects a wide range of plants, causing characteristic mosaic-like patterns, especially on tobacco leaves, while it is completely harmless to mammals. Its structure and physical chemical properties are well known, but it is worthwhile mentioning its exceptional structural and chemical stability 57) even under extrem conditions, for example, at high temperatures, 56) in organic solvents, [58][59][60] and in a wide range of pH from acid to alkaline conditions. 61) Furthermore, TMV is a relevant example of how the supramolecular self-assembly of about 2000 proteins and an RNA strand can give rise to a nanoscale tubular architecture [Figs.…”

Hydrophobic Cargo Encapsulation into Virus Protein Cages by Self-Assembly in an Aprotic Organic Solvent

“…To the best of our knowledge, self-assembly of VLPs in DMSO-containing solutions has never been studied. Presumably, the known DMSO ability to inactivate viruses and denature certain proteins ,, has dampened the enthusiasm for such explorations. However, the capsids of many icosahedral plant viruses are stabilized by the hydrophobic effect, and previous computations suggest that the water hydrogen-bonding network should be minimally affected by mixing with DMSO .…”

The Effect of Urea on Tobacco Mosaic Virus: Polarity of Disassembly

“…Alkali (Perham & Wilson, 1976;Ohno & Okada, 1977;Pelcher & Halasa, 1979), SDS (Ohno & Okada, 1977;May & Knight, 1965;Wilson et al, 1976) or dimethyl sulphoxide (Nicolaieff & Lebeurier 1979;Wilson, 1978;Wilson et al, 1981) remove coat protein subunits from the virus RNA in a polar fashion, predominantly from the 5'-terminus. A small and variable number of rods are stripped bi-directionally by these agents; uncoating from the 3'-end appears to begin at a later stage and proceeds for a shorter distance .…”