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Viruses 2018, 10(2), 56;

Virus Infection Triggers MAVS Polymers of Distinct Molecular Weight

CRCHUM—Centre Hospitalier de l’Université de Montréal, 900 rue Saint Denis, Montréal, QC H2X 0A9, Canada
Department of Biochemistry and Molecular Medicine, Faculty of Medicine, Université de Montréal, Montréal, QC H3C 3J7, Canada
Author to whom correspondence should be addressed.
Received: 4 January 2018 / Revised: 24 January 2018 / Accepted: 26 January 2018 / Published: 30 January 2018
(This article belongs to the Section Animal Viruses)
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The mitochondrial antiviral signaling (MAVS) adaptor protein is a central signaling hub required for cells to mount an antiviral response following virus sensing by retinoic acid-inducible gene I (RIG-I)-like receptors. MAVS localizes in the membrane of mitochondria and peroxisomes and in mitochondrial-associated endoplasmic reticulum membranes. Structural and functional studies have revealed that MAVS activity relies on the formation of functional high molecular weight prion-like aggregates. The formation of protein aggregates typically relies on a dynamic transition between oligomerization and aggregation states. The existence of intermediate state(s) of MAVS polymers, other than aggregates, has not yet been documented. Here, we used a combination of non-reducing SDS-PAGE and semi-denaturing detergent agarose gel electrophoresis (SDD-AGE) to resolve whole cell extract preparations to distinguish MAVS polymerization states. While SDD-AGE analysis of whole cell extracts revealed the formation of previously described high molecular weight prion-like aggregates upon constitutively active RIG-I ectopic expression and virus infection, non-reducing SDS-PAGE allowed us to demonstrate the induction of lower molecular weight oligomers. Cleavage of MAVS using the NS3/4A protease revealed that anchoring to intracellular membranes is required for the appropriate polymerization into active high molecular weight aggregates. Altogether, our data suggest that RIG-I-dependent MAVS activation involves the coexistence of MAVS polymers with distinct molecular weights. View Full-Text
Keywords: mitochondrial antiviral signaling (MAVS); virus; antiviral; interferon; pathogen recognition receptors (PRRs); oligomerization; aggregation mitochondrial antiviral signaling (MAVS); virus; antiviral; interferon; pathogen recognition receptors (PRRs); oligomerization; aggregation

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Zamorano Cuervo, N.; Osseman, Q.; Grandvaux, N. Virus Infection Triggers MAVS Polymers of Distinct Molecular Weight. Viruses 2018, 10, 56.

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