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P Palese

Publications and source records attributed to P Palese.

At least 181 records · Page 10Linked to original sources

Temperature-sensitive mutants of influenza WSN virus defective in virus-specific RNA synthesis.

Influenza WSN virus temperature-sensitive (ts) mutants were examined for defects in viral complementary RNA (cRNA) synthesis. The synthesis of viral cRNA was determined by hybridizing RNA from infected cells to radiolabeled virion RNA of known specific activity. Mutants in complementation groups I and III synthesized little, or no, cRNA at the nonpermissive temperature (39.5 C). When cells infected by these mutants were incubated for 5 h at the permissive temperature (33 C) and were then shifted to 39.5 C, net synthesis of cRNA ceased. This strongly suggests that mutants in these two complementation groups possess a ts defect in the transciptase complex. Mutants in group II and group V synthesize reduced amounts of cRNA at 39.5 C. In contrast to the group I and group III mutants, cRNA synthesis in cells infected by a group II or a group V mutant continues after a shift-up. This indicated that these mutants do not possess a ts transcriptase complex and that these mutants are most probably defective in some step in the amplification of cRNA synthesis. As will be discussed, the most likely defect in these mutants is in the synthesis of virion-type RNA. These results suggest that there are two influenza viral gene functions required for transcription and most likely two additional gene functions required for RNA replication.

Cell Line↗

Applications of a synthetic neuraminidase substrate.

A rapid and precise assay for neuraminidase using 2-(3'-methoxyphenyl)-N-acetyl-alpha-neuraminic acid (MPN) is described. It is proposed that this substrate be used for the standardization of activity of neuraminidases from viral, bacterial, and mammalian sources. MPN is also used as a chromogenic substrate to localize influenza and parainfluenza virus foci in tissue culture. This technique permits the recovery of infective virus from these stained "plaques." It has also been demonstrated that immunoprecipitin lines containing neuraminidase complexes with antibody in the Ouchterlony test can be observed by a similar staining procedure. No enzyme inhibition occurs in the presence of anti-neuraminidase antibodies or concanavalin A when MPN is used as a substrate in contrast to the results with high-molecular-weight substrates such as fetuin.

Animals↗

Degradation of single- and double-stranded RNA by frog virus 3.

Purified preparations of frog virus 3 possess ribonuclease activities directed against single-and double-stranded RNA. Double-stranded RNAs isolated from purified reovirus type 3 and from HeLa cells infected with poliovirus and single-stranded poliovirus RNA from purified virus are readily degraded by incubation with frog virus 3. The mode of action of the nucleases is endonucleolytic. Under the assay conditions used for the viral enzyme, crude extracts of uninfected HeLa, L, and baby hamster kidney cells did not show enzyme activity against double-stranded RNA but exhibited activity against single-stranded RNA. The dependence of the viral nucleases on divalent cations for optimal activity and the inhibition of the cleavage of single-stranded RNA by 0.2 M NaCl suggests that the enzymes are either virus-coded or virus-induced.

Animals↗

Proteins of a polyhedral cytoplasmic deoxyvirus. 3. Structure of frog virus 3 and location ov virus-associated adenosine triphosphate phosphohydrolase.

The adenosine triphosphatase associated with frog virus 3 shows high specificity for ATP or deoxyadenosine triphosphate and appears to be distinct from the corresponding activity in host cells, poxvirus, or reovirus. The enzyme activity is probably integrated into virus particles since it is firmly associated with subviral particles produced when approximately 50 to 60% of the outer viral protein is removed by detergent treatment. The occurrence of adenosine triphosphatase activity within three unrelated viruses suggests that adenosine tryphosphatase might be a necessary function for most viruses that replicate in the cell cytoplasm.

Adenosine Triphosphatases↗

Germ of an idea.

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Aerosols↗

Polyacrylamide gel electrophoresis of the RNAs of new influenza virus strains: an epidemiological tool.

Recently, we have shown by separating the RNAs and proteins of different influenza A viruses on polyacrylamide gels, that influenza A viruses contain 8 genes corresponding to 8 virus specific proteins. By analyzing the RNA patterns and the protein patterns of different recombinant viruses we, subsequently, succeeded in establishing a complete genetic map for influenza A viruses. These techniques were extended to characterize the genome of new influenza virus isolates. Thus it was found that the human isolate A/Wi/263/76 and the two swine virus isolates, A/swine/Wi/49/76 and A/swine/Wi/50/76 possess identical RNA patterns, which differ from the RNA patterns of other recent swine virus isolates. The human (Wi/263) and the two animal isolates (Wi/49 and Wi/50) were obtained on the same farm suggesting that the animal virus was transmitted from swine to man. This proves that swine viruses may occasionally infect humans without causing a pandemic. A comparative analysis of the different RNA patterns of other swine influenza viruses isolated around the same time at different locations and of those of recent human isolates showed that our polyacrylamide gel technique is a valuable epidemiological tool to identify and and characterize different influenza virus isolates.

Animals↗