Specific Nucleoprotein Residues Affect Influenza Virus Morphology
| Autor: | Kristy M. Bialas, Kendra A. Bussey, Toru Takimoto, Raychel Stone |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Kobuvirus
viruses Blotting Western Immunology M1 protein Molecular Conformation Hemagglutinin (influenza) medicine.disease_cause Microbiology Madin Darby Canine Kidney Cells Viral Matrix Proteins Dogs Virology Virus morphology Influenza A virus medicine Animals Humans Immunoprecipitation Viral matrix protein biology Structure and Assembly virus diseases biochemical phenomena metabolism and nutrition biology.organism_classification Molecular biology Nucleoprotein HEK293 Cells Nucleoproteins Microscopy Fluorescence Insect Science Microscopy Electron Scanning Mutagenesis Site-Directed biology.protein Hybridization Genetic RNA Aichi virus Neuraminidase |
| Zdroj: | Journal of Virology. 88:2227-2234 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.03354-13 |
| Popis: | Influenza virus strains are often pleiomorphic, a characteristic that is largely attributed to specific residues in matrix protein 1 (M1). Although the mechanism by which M1 controls virion morphology has not yet been defined, it is suggested that the M1 interaction with other viral proteins plays an important role. In this study, we rescued recombinant virus WSN-AichiM1 containing the spherical A/WSN/33 (WSN) backbone and the M1 protein from A/Aichi/2/68 (Aichi). Aichi M1 differs from WSN M1 by 7 amino acids but includes those identified to be responsible for filamentous virion formation. Interestingly, Aichi virus produced spherical virions, while WSN-AichiM1 exhibited a long filamentous morphology, as detected by immunofluorescence and electron microscopy. Additional incorporation of Aichi nucleoprotein (NP) but not the hemagglutinin (HA), neuraminidase (NA), or M2 gene to WSN-AichiM1 abrogated filamentous virion formation, suggesting that specific M1-NP interactions affect virion morphology. Further characterization of viruses containing WSN/Aichi chimeric NPs identified residues 214, 217, and 253 of Aichi NP as necessary and sufficient for the formation of spherical virions. NP residues 214 and 217 localize at the minor groove between the two opposite-polarity NP helical strands of viral ribonucleocapsids, and residue 253 also localizes near the surface of the groove. These findings indicate that NP plays a critical role in influenza virus morphology, possibly through its interaction with the M1 layer during virus budding. |
| Databáze: | OpenAIRE |
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