ArticleJournal of virology2008
Human respiratory syncytial virus glycoproteins are not required for apical targeting and release from polarized epithelial cells.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed.
- Article
- The Morphology and Assembly of Respiratory Syncytial Virus Revealed by Cryo-Electron Tomography.Viruses · 2018Article
- Article
- The Respiratory Syncytial Virus Phosphoprotein, Matrix Protein, and Fusion Protein Carboxy-Terminal Domain Drive Efficient Filamentous Virus-Like Particle Formation.Journal of virology · 2016Article
- Fluorescent and Bioluminescent Reporter Myxoviruses.Viruses · 2016Review
- iTRAQ-based comparative proteomic analysis of Vero cells infected with virulent and CV777 vaccine strain-like strains of porcine epidemic diarrhea virus.Journal of proteomics · 2016Article
- Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Viruses · 2014Review
- Article
- The respiratory syncytial virus fusion protein targets to the perimeter of inclusion bodies and facilitates filament formation by a cytoplasmic tail-dependent mechanism.Journal of virology · 2013Article
- RSV fusion: time for a new model.Viruses · 2013Review
- Nipah virus entry and egress from polarized epithelial cells.Journal of virology · 2013Article
- Host and Viral Factors in Respiratory Syncytial Virus Infection.Current pediatrics reports · 2013Article
- The human respiratory syncytial virus matrix protein is required for maturation of viral filaments.Journal of virology · 2012Article
- Article
- Evaluation of the Calu-3 cell line as a model of in vitro respiratory syncytial virus infection.Journal of virological methods · 2011Article
- Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells.Advances in virology · 2011Article
- Quantitative proteomics using stable isotope labeling with amino acids in cell culture reveals changes in the cytoplasmic, nuclear, and nucleolar proteomes in Vero cells infected with the coronavirus infectious bronchitis virus.Molecular & cellular proteomics : MCP · 2010Article
- Paramyxovirus assembly and budding: building particles that transmit infections.The international journal of biochemistry & cell biology · 2010Review
- Viral protein determinants of Lassa virus entry and release from polarized epithelial cells.Journal of virology · 2010Article
- Herpes simplex virus type 1 glycoprotein E mediates retrograde spread from epithelial cells to neurites.Journal of virology · 2009Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Human respiratory syncytial virus (HRSV) is released from the apical membrane of polarized epithelial cells. However, little is known about the processes of assembly and release of HRSV and which viral gene products are involved in the directional maturation of the virus. Based on previous studies showing that the fusion (F) glycoprotein contained an intrinsic apical sorting signal and that N- and O-linked glycans can act as apical targeting signals, we investigated whether the glycoproteins of HRSV were involved in its directional targeting and release. We generated recombinant viruses with each of the three glycoprotein genes deleted individually or in groups. Each deleted gene was replaced with a reporter gene to maintain wild-type levels of gene expression. The effects of deleting the glycoprotein genes on apical maturation and on targeting of individual proteins in polarized epithelial cells were examined by using biological, biochemical, and microscopic assays. The results of these studies showed that the HRSV glycoproteins are not required for apical maturation or release of the virus. Further, deletion of one or more of the glycoprotein genes did not affect the intracellular targeting of the remaining viral glycoproteins or the nucleocapsid protein to the apical membrane.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.