Abstract
It was shown previously that the matrix (M), phosphoprotein (P), and fusion (F) proteins of respiratory syncytial virus (RSV) are sufficient to produce virus-like particles (VLPs) that resemble the RSV infection-induced virions. However, the exact mechanism and interactions among the three proteins are not known. This work examines the interaction between P and M during RSV assembly and budding. We show that M interacts with P in the absence of other viral proteins in cells by using a split Nano luciferase assay. By using recombinant proteins, we demonstrate a direct interaction between M and P. By using nuclear magnetic resonance (NMR), we identify three novel M interaction sites on P, namely, site I in the αN2 region, site II in the 115 to 125 region, and the oligomerization domain (OD). We show that the OD, and likely the tetrameric structural organization of P, is required for virus-like filament formation and VLP release. Although sites I and II are not required for VLP formation, they appear to modulate P levels in RSV VLPs.
| Original language | English |
|---|---|
| Article number | e02217-20 |
| Number of pages | 20 |
| Journal | Journal of Virology |
| Volume | 95 |
| Issue number | 7 |
| Early online date | 10 Mar 2021 |
| DOIs | |
| Publication status | Published - Apr 2021 |
Funding
We thank Benoit Maury and CYMAGES imaging facility (Département Biotechnologie Santé, Université Versailles Saint Quentin, France) for their support and assistance with the confocal imaging. We thank Damien Vitour (E’quipe du Laboratoire d'Immunologie de Seppic) and the animal facilities (ANSES Maisons-Alfort) for rabbit immunization with recombinant M. This work was carried out with the financial support of the French Agence Nationale de la Recherche DecRisP (ANR-19_CE11_0017).