ArticleVirology2019
Identification of a human respiratory syncytial virus phosphoprotein domain required for virus-like-particle formation.
Article in Virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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
6 citing papers in PubMed.
- Epidemiological characteristics and whole-genome analysis of respiratory syncytial virus in Jining city from February 2023 to December 2024.Frontiers in microbiology · 2026Article
- Article
- Article
- Role of VP30 Phosphorylation in Ebola Virus Nucleocapsid Assembly and Transport.Journal of virology · 2022Article
- Respiratory syncytial virus ribonucleoproteins hijack microtubule Rab11 dependent transport for intracellular trafficking.PLoS pathogens · 2022Article
- Tetramerization of Phosphoprotein is Essential for Respiratory Syncytial Virus Budding while its N Terminal Region Mediates Direct Interactions with the Matrix Protein.Journal of virology · 2021Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Perceived inefficiency and inadequate knowledge of the human respiratory syncytial virus (hRSV) assembly process present a hurdle for large-scale production of authentic hRSV virus-like particles (VLPs) for vaccine purposes. We previously established that the matrix protein, phosphoprotein (P), and fusion protein carboxy-terminus were sufficient to generate VLPs that resemble filamentous wildtype hRSV. Here, the contribution of P was examined. By co-expressing matrix, fusion, and modified P proteins, a ser/thr-rich P region (residues 39-57) was found to be critical for VLP formation, whereas the oligomerization domain was not. Substitutions throughout region 39-57 inhibited VLP formation and relevant amino acids were identified. Phosphomimetic substitutions of serines and threonines inhibited VLP formation; Phosphoblatant substitutions did not. The data show that P not only co-regulates replication and transcription but also has an important role in assembly, mediated by a separate domain that likely interacts with M and/or F and is highly regulated by phosphorylation.
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Registered trials
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