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• W2940374012 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." @default.
• W2940374012 created "2019-04-25" @default.
• W2940374012 creator A5002386886 @default.
• W2940374012 creator A5061397335 @default.
• W2940374012 date "2019-06-01" @default.
• W2940374012 modified "2023-10-16" @default.
• W2940374012 title "Identification of a human respiratory syncytial virus phosphoprotein domain required for virus-like-particle formation" @default.
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• W2940374012 doi "https://doi.org/10.1016/j.virol.2019.04.001" @default.
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