Virus Infection Triggers MAVS Polymers of Distinct Molecular Weight
| Autor: | Quentin Osseman, Nathalie Grandvaux, Natalia Zamorano Cuervo |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Polymers lcsh:QR1-502 mitochondrial antiviral signaling (MAVS) virus antiviral interferon pathogen recognition receptors (PRRs) oligomerization aggregation Viral Nonstructural Proteins Protein aggregation Respirovirus Infections Sendai virus lcsh:Microbiology Article Protein Aggregates 03 medical and health sciences Cell Line Tumor Virology Humans Receptors Immunologic Adaptor Proteins Signal Transducing Electrophoresis Agar Gel NS3 Molecular mass biology Chemistry Endoplasmic reticulum HEK 293 cells Signal transducing adaptor protein Intracellular Membranes biology.organism_classification Mitochondria Cell biology Molecular Weight HEK293 Cells 030104 developmental biology Infectious Diseases DEAD Box Protein 58 Serine Proteases Intracellular |
| Zdroj: | Viruses; Volume 10; Issue 2; Pages: 56 Viruses Viruses, Vol 10, Iss 2, p 56 (2018) |
| ISSN: | 1999-4915 |
| DOI: | 10.3390/v10020056 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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