Oligomerization and Cell Egress Controlled by Two Microdomains of Canine Distemper Virus Matrix Protein.
M-M interaction
VLPs production
dynamics at the cell surface
matrix protein
morbillivirus cell exit
Journal
mSphere
ISSN: 2379-5042
Titre abrégé: mSphere
Pays: United States
ID NLM: 101674533
Informations de publication
Date de publication:
14 04 2021
14 04 2021
Historique:
entrez:
15
4
2021
pubmed:
16
4
2021
medline:
29
10
2021
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 33853875
pii: 6/2/e01024-20
doi: 10.1128/mSphere.01024-20
pmc: PMC8546710
pii:
doi:
Substances chimiques
Glycoproteins
0
Viral Proteins
0
protein M (glycoprotein)
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2021 Gast et al.
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