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Biomedical subjects

E Wimmer

Publications and source records attributed to E Wimmer.

264 records · Page 15Linked to original sources

Polyadenylic acid at the 3'-terminus of poliovirus RNA.

Poliovirus RNA that has been derivatized at the 3'-end with NaIO(4)-NaB(3)H(4) yields, after hydrolysis with alkali or RNase T2, predominantly labeled residues of modified adenosine; no labeled nucleoside derivative is produced by digestion with RNase A or RNase T1. The 3'-terminal bases of the RNA are, therefore,...ApA(OH). Hydrolyzates of poliovirus [(32)P]RNA, after exhaustive digestion with RNase T1 or RNase A, contain, besides internal oligonucleotides, polynucleotides resistant to further action of ribonucleases T1 and A, respectively; these polynucleotides were isolated by membrane-filter binding or ion-exchange chromatography. The sequence of the T1-resistant polynucleotide was determined to be (Ap)(n)A(OH), that of the RNase A-resistant polynucleotide was GpGp(Ap)(n)A(OH). The chain length (n) of the polyadenylic acid, as analyzed by different methods, averages 89 nucleotides. Gel electrophoresis revealed heterogeneity of the size of poly(A). Poliovirus RNA, when labeled in vitro at the 3'-end, contains [3'-(3)H]poly(A); when labeled in vivo with [(3)H]A, it contains [(3)H](Ap)(n)A(OH). The data establish that... YpGpGp(Ap)([unk])A(OH) is the 3'-terminal sequence of poliovirus RNA, Type 1 (Mahoney). Since this mammalian virus reproduces in the cell cytoplasm, these observations may modify prior interpretations of the function of polyadenylate ends on messenger RNAs.

Adenine Nucleotides↗

Defective interfering particles of poliovirus. I. Isolation and physical properties.

A class of defective interfering (DI) poliovirus particles has been identified. The first was found as a contaminant of a viral stock; others have been isolated by serial passage at a high multiplicity of infection. The DI particles are less dense than standard virus and sediment more slowly. Their ribonucleic acid (RNA) sediments more slowly than standard RNA and has a higher electrophoretic mobility. Competition hybridization experiments with double-stranded viral RNA indicate that DI RNA is 80 to 90% of the length of standard RNA. The proteins of DI particles are indistinguishable from those of standard poliovirus.

Carbon Isotopes↗

Pyrophosphate in the 5' terminal position of a viral ribonucleic acid.

A pancreatic ribonuclease digest of carbon-14-labeled Satellite Tobacco Necrosis Virus RNA was fractionated, according to charge, by column chromatography. Individual fractions were dephosphorylated with alkaline phosphomonoesterase and rechromatogramed. The fraction originally containing oligonucleotides with seven negative charges separated into two components corresponding to five and two negative charges, respectively, and therefore must have contained a terminal trinucleotide 5'-pyrophosphate, in addition to the internal hexanucleotides. Other fractions when similarly treated were found to contain only internal oligonucleotides.

Alkaline Phosphatase↗

Priming for and induction of anti-poliovirus neutralizing antibodies by synthetic peptides.

Five peptides containing amino acid sequences from the type 1 poliovirus structural protein VP1 have been synthesized. Each of the peptides was found capable of priming the immune system of rabbits for a long-lasting, virus-neutralizing IgG antibody response following a single inoculation of intact virus. One peptide directly induced the production of neutralizing antibody.

Amino Acid Sequence↗

Peptide priming of a poliovirus neutralizing antibody response.

Two peptides representing neutralizing epitope-containing regions of the capsid protein VP1 of type 1 poliovirus were chemically synthesized. Both peptides were found capable of priming rabbits for a significant, long-lasting, anti-virus neutralizing IgG response following a single inoculation of intact virion. In addition, a third synthetic peptide, an extended version of one of the two priming peptides, was capable of eliciting a neutralizing antibody response following inoculation of the carrier-linked peptide alone.

Animals↗