Palmitoylation is required for intracellular trafficking of influenza B virus NB protein and efficient influenza B virus growth in vitro
| Autor: | Dan Wang, Andrew Demers, Brody Edman, Feng Li, Zhiguang Ran, Wuxun Lu, Qiji Deng |
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| Rok vydání: | 2014 |
| Předmět: |
Genes
Viral Lipoylation Golgi Apparatus Biology Endoplasmic Reticulum Virus Replication Cell membrane Viral Proteins chemistry.chemical_compound symbols.namesake Palmitoylation Virology Chlorocebus aethiops medicine Animals Cysteine Lipid raft Secretory pathway Animal Endoplasmic reticulum Cell Membrane Brefeldin A Golgi apparatus Protein Structure Tertiary Transport protein Influenza B virus Protein Transport medicine.anatomical_structure Amino Acid Substitution chemistry COS Cells Mutagenesis Site-Directed symbols |
| Zdroj: | Journal of General Virology. 95:1211-1220 |
| ISSN: | 1465-2099 0022-1317 |
| DOI: | 10.1099/vir.0.063511-0 |
| Popis: | All influenza viruses bud and egress from lipid rafts within the apical plasma membrane of infected epithelial cells. As a result, all components of progeny virions must be transported to these lipid rafts for assembly and budding. Although the mechanism of transport for other influenza proteins has been elucidated, influenza B virus (IBV) glycoprotein NB subcellular localization and transport are not understood completely. To address the aforementioned properties of NB, a series of trafficking experiments were conducted. Here, we showed that NB co-localized with markers specific for the endoplasmic reticulum (ER) and Golgi region. The data from chemical treatment of NB-expressing cells by Brefeldin A, a fungal antibiotic and a known chemical inhibitor of the protein secretory pathway, further confirmed that NB is transported through the ER–Golgi pathway as it restricted NB localization to the perinuclear region. Using NB deletion mutants, the hydrophobic transmembrane domain was identified as being required for NB transport to the plasma membrane. Furthermore, palmitoylation was also required for transport of NB to the plasma membrane. Systematic mutation of cysteines to serines in NB demonstrated that cysteine 49, likely in a palmitoylated form, is also required for transport to the plasma membrane. Surprisingly, further analysis demonstrated thatin vitroreplication of NBC49S mutant virus was delayed relative to the parental IBV. The results demonstrated that NB is the third influenza virus protein to have been shown to be palmitoylated and together these findings may aid in future studies aimed at elucidating the function of NB. |
| Databáze: | OpenAIRE |
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