Vaccines: a study in contrasts.
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Biomedical subjects
Publications and source records attributed to P A Kiberstis.
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Solanum nodiflorum mottle virus (SNMV) RNA2 is a single-stranded, covalently closed circular molecule. RNase T2 or nuclease P1 digests of this RNA contain a minor nucleotide of unusual chromatographic and electrophoretic mobility. This nucleotide is resistant to further digestion by T2 or P1 ribonucleases, or by alkali, but is sensitive to venom phosphodiesterase digestion. Alkaline phosphatase digestion yields a product which is RNase T2 and P1 sensitive. The products of these various digests show that the minor nucleotide is a ribonuclease-resistant dinucleotide carrying a 2' phosphomonoester group with the core structure C2'p3'p5'A. This dinucleotide is found in a unique RNase T1 product of SNMV RNA2, thus establishing a unique location in the sequence for the 2' phosphomonoester group at residue 49. Identical results have been obtained with a second related virus. The phosphomonoester group probably results from the RNA ligation event by which the molecules were circularised.
Solanum nodiflorum mottle virus RNA (Mr = 1.5 X 10(6)) was translated in vitro in a wheat embryo extract. Four major products were synthesized: 2 related proteins of molecular weight 100K (P100) and 67K (P67), a protein of molecular weight 38K (P38), and a methionine-lacking protein of molecular weight 28K (P28). P38 was synthesized by a minor RNA component (Mr approximately 0.4 X 10(6)) and comigrated with the only viral product detected in SNMV-infected N. clevelandii protoplasts. Antiserum raised against purified SNMV virions precipitated both in vitro- and in vivo-synthesized P38, suggesting that it is either a precursor to or an intact form of SNMV coat protein whose apparent molecular weight in purified virus preparations is 30K.