Protein lysine acetylation involved in the antiviral innate immunity contributes to the regulation of antiviral inflammation responses, including type 1 interferon production and interferon-stimulated gene expression. Thus, investigation of acetylated antiviral proteins is vital for the complete understanding of inflammatory responses to viral infections. Immunoprecipitation (IP) assay with anti-targeted-protein antibody or with acetyl-lysine affinity beads followed by immunoblot provides a classical way to determine the potential modified protein in the antiviral innate pathways, whereas mass spectrometry can be utilized to identify the accurate acetylation lysine residues or explore the acetyl-proteomics. We demonstrate here comprehensive methods of protein lysine acetylation determination in virus-infected macrophages and embryonic fibroblast cells or proteins-overexpressed HEK 293 T cells in the context of antiviral innate immunity.
Keyphrases
- amino acid
- mass spectrometry
- gene expression
- protein protein
- binding protein
- immune response
- sars cov
- histone deacetylase
- dna methylation
- induced apoptosis
- high throughput
- cell proliferation
- ms ms
- cell death
- cell cycle arrest
- capillary electrophoresis
- climate change
- cancer therapy
- label free
- simultaneous determination