Next Article in Journal
Calcitriol Inhibits HCV Infection via Blockade of Activation of PPAR and Interference with Endoplasmic Reticulum-Associated Degradation
Previous Article in Journal
CRISPR–Cas9 Genetic Analysis of Virus–Host Interactions
Article Menu
Issue 2 (February) cover image

Export Article

Open AccessArticle
Viruses 2018, 10(2), 56; https://doi.org/10.3390/v10020056

Virus Infection Triggers MAVS Polymers of Distinct Molecular Weight

1
CRCHUM—Centre Hospitalier de l’Université de Montréal, 900 rue Saint Denis, Montréal, QC H2X 0A9, Canada
2
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)
View Full-Text   |   Download PDF [4680 KB, uploaded 30 January 2018]   |  

Abstract

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
Figures

Graphical abstract

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).
SciFeed

Share & Cite This Article

MDPI and ACS Style

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

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Viruses EISSN 1999-4915 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top