Tetramerization of Phosphoprotein Is Essential for Respiratory Syncytial Virus Budding while Its N-Terminal Region Mediates Direct Interactions with the Matrix Protein
Monika Bajorek, Marie Galloux, Charles-Adrien Richard, Or Szekely, Rina Rosenzweig, Christina Sizun, Jean‐François Eléouët
Abstract
Human RSV is the commonest cause of infantile bronchiolitis in the developed world and of childhood deaths in resource-poor settings. It is a major unmet target for vaccines and anti-viral drugs. The lack of knowledge of RSV budding mechanism presents a continuing challenge for VLP production for vaccine purpose. We show that direct interaction between P and M modulates RSV VLP budding. This further emphasizes P as a central regulator of RSV life cycle, as an essential actor for transcription and replication early during infection and as a mediator for assembly and budding in the later stages for virus production.
Topics & Concepts
PhosphoproteinBiologyViral matrix proteinVirusBuddingVirologyCell biologyBinding siteFusion proteinRecombinant DNAPhosphorylationGeneticsGeneRespiratory viral infections researchCongenital Diaphragmatic Hernia StudiesViral Infections and Vectors