Temperature-Sensitive Lesions in Two Influenza A Viruses Defective for Replicative Transcription Disrupt RNA Binding by the Nucleoprotein
| Autor: | Liz Medcalf, Paul Digard, Emma Poole, Debra Elton |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Influenza A virus/physiology
Transcription Genetic viruses Immunology Replication Virus Replication medicine.disease_cause Microbiology Defective virus Virus Cell Line Cercopithecus aethiops Transcription (biology) Cricetinae Virology Chlorocebus aethiops Influenza A virus medicine Animals Humans RNA Viral/biosynthesis Influenza A virus/genetics Polymerase biology Viral Core Proteins Defective Viruses/physiology Nucleoproteins/metabolism Temperature Viral Core Proteins/metabolism Defective Viruses RNA-Binding Proteins RNA Nucleocapsid Proteins Molecular biology Nucleoprotein Nucleoproteins Viral replication Insect Science biology.protein RNA Viral Defective Viruses/genetics |
| Zdroj: | Europe PubMed Central Medcalf, L, Poole, E, Elton, D & Digard, P 1999, ' Temperature-sensitive lesions in two influenza A viruses defective for replicative transcription disrupt RNA binding by the nucleoprotein ', Journal of Virology, vol. 73, no. 9, pp. 7349-56 . < http://jvi.asm.org/content/73/9/7349.long > |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.73.9.7349-7356.1999 |
| Popis: | The negative-sense segmented RNA genome of influenza virus is transcribed into capped and polyadenylated mRNAs, as well as full-length replicative intermediates (cRNAs). The mechanism that regulates the two forms of transcription remains unclear, although several lines of evidence imply a role for the viral nucleoprotein (NP). In particular, temperature-shift and biochemical analyses of the temperature-sensitive viruses A/WSN/33 ts 56 and A/FPV/Rostock/34/Giessen ts G81 containing point mutations within the NP coding region have indicated specific defects in replicative transcription at the nonpermissive temperature. To identify the functional defect, we introduced the relevant mutations into the NP of influenza virus strain A/PR/8/34. Both mutants were temperature sensitive for influenza virus gene expression in transient-transfection experiments but localized and accumulated normally in transfected cells. Similarly, the mutants retained the ability to self-associate and interact with the virus polymerase complex whether synthesized at the permissive or the nonpermissive temperatures. In contrast, the mutant NPs were defective for RNA binding when expressed at the nonpermissive temperature but not when expressed at 30°C. This suggests that the RNA-binding activity of NP is required for replicative transcription. |
| Databáze: | OpenAIRE |
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