@article{9361,
  abstract     = {The multimeric matrix (M) protein of clinically relevant paramyxoviruses orchestrates assembly and budding activity of viral particles at the plasma membrane (PM). We identified within the canine distemper virus (CDV) M protein two microdomains, potentially assuming α-helix structures, which are essential for membrane budding activity. Remarkably, while two rationally designed microdomain M mutants (E89R, microdomain 1 and L239D, microdomain 2) preserved proper folding, dimerization, interaction with the nucleocapsid protein, localization at and deformation of the PM, the virus-like particle formation, as well as production of infectious virions (as monitored using a membrane budding-complementation system), were, in sharp contrast, strongly impaired. Of major importance, raster image correlation spectroscopy (RICS) revealed that both microdomains contributed to finely tune M protein mobility specifically at the PM. Collectively, our data highlighted the cornerstone membrane budding-priming activity of two spatially discrete M microdomains, potentially by coordinating the assembly of productive higher oligomers at the PM.},
  author       = {Gast, Matthieu and Kadzioch, Nicole P. and Milius, Doreen and Origgi, Francesco and Plattet, Philippe},
  issn         = {23795042},
  journal      = {mSphere},
  number       = {2},
  publisher    = {American Society for Microbiology},
  title        = {{Oligomerization and cell egress controlled by two microdomains of canine distemper virus matrix protein}},
  doi          = {10.1128/mSphere.01024-20},
  volume       = {6},
  year         = {2021},
}