tetano
Editor, Senior Moderator
J Gen Virol. 2014 Mar 26. doi: 10.1099/vir.0.063511-0. [Epub ahead of print]
Palmitoylation Is Required for Intracellular Trafficking of Influenza B Virus NB Protein and Efficient Influenza B Growth In Vitro.
Demers AJ1, Ran Z, Deng Q, Wang D, Edman B, Lu W, Li F.
Author information
Abstract
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 lipids rafts for assembly and budding. Though the mechanism of transport for other influenza proteins has been elucidated, influenza B glycoprotein NB subcellular localization and transport are not completely understood. To address the aforementioned properties of NB protein, a series of trafficking experiments were conducted. Here we showed that NB co-localized with markers specific for the endoplasmic reticulum 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 protein to the plasma membrane. Systematic mutation of NB's cysteines to serines demonstrated that cysteine 49, likely in a palmitoylated form, is also required for transport to the plasma membrane. Surprisingly, further analysis demonstrated that in vitro replication of NBC49S mutant virus was delayed relative to the parental influenza B virus. The results of this study demonstrate 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 NB's function.
KEYWORDS:
Influenza B, NB Protein, Palmitoylation
PMID:
24671751
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24671751
Palmitoylation Is Required for Intracellular Trafficking of Influenza B Virus NB Protein and Efficient Influenza B Growth In Vitro.
Demers AJ1, Ran Z, Deng Q, Wang D, Edman B, Lu W, Li F.
Author information
Abstract
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 lipids rafts for assembly and budding. Though the mechanism of transport for other influenza proteins has been elucidated, influenza B glycoprotein NB subcellular localization and transport are not completely understood. To address the aforementioned properties of NB protein, a series of trafficking experiments were conducted. Here we showed that NB co-localized with markers specific for the endoplasmic reticulum 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 protein to the plasma membrane. Systematic mutation of NB's cysteines to serines demonstrated that cysteine 49, likely in a palmitoylated form, is also required for transport to the plasma membrane. Surprisingly, further analysis demonstrated that in vitro replication of NBC49S mutant virus was delayed relative to the parental influenza B virus. The results of this study demonstrate 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 NB's function.
KEYWORDS:
Influenza B, NB Protein, Palmitoylation
PMID:
24671751
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24671751