Functional organization of cytoplasmic inclusion bodies in cells infected by respiratory syncytial virus
نویسندگان
چکیده
منابع مشابه
Observation of Inclusion Bodies in Renal Epithelial Cells of Experimelltally Infected Horses with African Horse-Sickness Virus
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Analysis of proteins synthesized in respiratory syncytial virus-infected cells.
The spectrum of respiratory syncytial virus-encoded proteins was examined in infected cell extracts by standard polyacrylamide gel electrophoresis and by two-dimensional gel analysis. Polyacrylamide gel electrophoresis analysis of a variety of respiratory syncytial virus-infected, actinomycin D-treated cell lines revealed the presence of as many as nine virus-encoded proteins. Seven of these ni...
متن کاملEpithelial Cells Induce Eosinophil Degranulation Respiratory Syncytial Virus-Infected Pulmonary
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p38 and OGT sequestration into viral inclusion bodies in cells infected with human respiratory syncytial virus suppresses MK2 activities and stress granule assembly.
Respiratory syncytial virus (RSV) forms cytoplasmic inclusion bodies (IBs) that are thought to be sites of nucleocapsid accumulation and viral RNA synthesis. The present study found that IBs also were the sites of major sequestration of two proteins involved in cellular signaling pathways. These are phosphorylated p38 mitogen-activated protein kinase (MAPK) (p38-P), a key regulator of cellular ...
متن کاملThe respiratory syncytial virus fusion protein targets to the perimeter of inclusion bodies and facilitates filament formation by a cytoplasmic tail-dependent mechanism.
The human respiratory syncytial virus (HRSV) fusion (F) protein cytoplasmic tail (CT) and matrix (M) protein are key mediators of viral assembly, but the underlying mechanisms are poorly understood. A complementation assay was developed to systematically examine the role of the F protein CT in infectious virus production. The ability of F mutants with alanine substitutions in the CT to compleme...
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ژورنال
عنوان ژورنال: Nature Communications
سال: 2017
ISSN: 2041-1723
DOI: 10.1038/s41467-017-00655-9