Proteasomes raise the microtubule dynamics in influenza A (H1N1) virus-infected LLC-MK2 cells
| Autor: | Alessandra Fazzi, Maria Cristina Arcangeletti, Sergey V. Razin, Carlo Chezzi, Flora De Conto, Adriana Calderaro, Maria Cristina Medici, Rita Gatti |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Proteasome Endopeptidase Complex
Pyrrolidines Leupeptins viruses Cell Biology Protein degradation medicine.disease_cause Virus Replication Biochemistry Microtubules Virus Cell Line Madin Darby Canine Kidney Cells chemistry.chemical_compound Dogs Influenza A Virus H1N1 Subtype Tubulin MG132 medicine Influenza A virus Animals Humans Pyrroles Molecular Biology Cytoskeleton Cell Proliferation Microscopy Confocal virus diseases Acetylation Cell Biology Virology Macaca mulatta medicine.anatomical_structure Viral replication Proteasome chemistry Cellular model Proteasome Inhibitors |
| Zdroj: | Cellularmolecular biology letters. 20(5) |
| ISSN: | 1689-1392 |
| Popis: | The dynamics of microtubule networks are known to have an impact on replication of influenza A virus in some cellular models. Here we present evidence suggesting that at late stages of LLC-MK2 cell infection by influenza A (H1N1) virus the ubiquitin-proteasome protein degradation system participates in destabilization of microtubules, and favours virus replication. Chemical inhibition of proteasome activity partially suppresses influenza A virus replication, while stimulation of proteasome activity favours influenza A virus replication. Conversely, in another cellular model, A549 cells, inhibitors and activators of proteasomes have a small effect on influenza A virus replication. These data suggest that influenza A virus might take selective advantage of proteasome functions in order to set up a favourable cytoskeletal “environment” for its replication and spread. Furthermore, the relationship between influenza virus and the host cell is likely to depend on both the cellular model and the virus strain. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink