ArticlePLoS pathogens2021
The larger attachment glycoprotein of respiratory syncytial virus produced in primary human bronchial epithelial cultures reduces infectivity for cell lines.
Article in PLoS pathogens, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 42 citations in OpenAlex.
- Cell culture medium influences RSV G protein glycosylation and recognition by monoclonal antibodies.Virology journal · 2026Article
- Gingipain proteases from the bacteriumProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Efficient replication of influenza D virus in the human airway underscores zoonotic potential.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Review
- Efficient replication of influenza D virus in the human airway underscores zoonotic potential.bioRxiv : the preprint server for biology · 2026Article
- Unraveling the dual immunomodulatory and immunogenic roles of the central conserved cysteine-rich region in respiratory syncytial virus G protein.Frontiers in microbiology · 2026Article
- Post-Translational Modifications in Respiratory Virus Infection: Recent Insights into the Development of In Vitro Models.International journal of molecular sciences · 2025Review
- Cytokine responses to respiratory syncytial virus infection in well-differentiated infant nasal epithelial cell cultures.Clinical and experimental vaccine research · 2025Article
- Preferential apical infection and spread of human metapneumovirus highlights the importance of inhaled delivery of neutralizing monoclonal antibody to treat established infections.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Host Immune Response to Respiratory Syncytial Virus Infection in Children.Influenza and other respiratory viruses · 2025Review
- RSV F evolution escapes some monoclonal antibodies but does not strongly erode neutralization by human polyclonal sera.Journal of virology · 2025Article
- Respiratory Syncytial Virus: A Narrative Review of Updates and Recent Advances in Epidemiology, Pathogenesis, Diagnosis, Management and Prevention.Journal of clinical medicine · 2025Review
- Advances in development of antiviral strategies against respiratory syncytial virus.Acta pharmaceutica Sinica. B · 2025Review
- Neuregulin-1 prevents death from a normally lethal respiratory viral infection.PLoS pathogens · 2025Article
- RSV F evolution escapes some monoclonal antibodies but does not strongly erode neutralization by human polyclonal sera.bioRxiv : the preprint server for biology · 2025Article
- Well-Differentiated Primary Human Airway Epithelial Cultures for Respiratory Syncytial Virus (RSV) Infection Studies.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Respiratory syncytial virus glycoprotein G impedes CXNpj viruses · 2024Article
- Virus neutralization assays for human respiratory syncytial virus using airway organoids.Cellular and molecular life sciences : CMLS · 2024Article
- Assessing the protection elicited by virus-like particles expressing the RSV pre-fusion F and tandem repeated G proteins against RSV rA2 line19F infection in mice.Respiratory research · 2024Article
- Respiratory syncytial virus infection and novel interventions.Nature reviews. Microbiology · 2023Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Respiratory syncytial virus (RSV) infects the upper and lower respiratory tracts and can cause lower respiratory tract infections in children and elders. RSV has traditionally been isolated, grown, studied and quantified in immortalized cell lines, most frequently HEp-2 cells. However, in vivo RSV infection is modeled more accurately in primary well differentiated human bronchial epithelial (HBE) cultures where RSV targets the ciliated cells and where the putative RSV receptor differs from the receptor on HEp-2 cells. The RSV attachment (G) glycoprotein in virions produced by HEp-2 cells is a highly glycosylated 95 kDa protein with a 32 kDa peptide core. However, virions produced in HBE cultures, RSV (HBE), contain an even larger, 170 kDa, G protein (LgG). Here we show that LgG is found in virions from both subgroups A and B lab-adapted and clinical isolates. Unexpectedly, RSV (HBE) virions were approximately 100-fold more infectious for HBE cultures than for HEp-2 cells. Surprisingly, the cause of this differential infectivity, was reduced infectivity of RSV (HBE) on HEp-2 cells rather than enhanced infectivity on HBE cultures. The lower infectivity of RSV(HBE) for HEp-2 cells is caused by the reduced ability of LgG to interact with heparan sulfate proteoglycans (HSPG), the RSV receptor on HEp-2 cells. The discovery of different infectivity corresponding with the larger form of the RSV attachment protein when produced by HBE cultures highlights the importance of studying a virus produced by its native host cell and the potential impact on quantifying virus infectivity on cell lines where the virus entry mechanisms differ from their natural target cell.
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Registered trials
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