Quantitative analysis of acetylation in peste des petits ruminants virus-infected Vero cells

• Published in: Virology journal 2023-10, Vol.20 (1), p.1-227, Article 227
• Main Authors: Meng, Xuelian, Wang, Xiangwei, Zhu, Xueliang, Zhang, Rui, Zhang, Zhidong, Sun, Yuefeng
• Format: Article
• Language: English
• Subjects: Acetylation; Amino acids; Antibodies; Care and treatment; Cytoplasm; Diseases; DNA helicase; Endoplasmic reticulum; Enzymes; Ethylenediaminetetraacetic acid; Health aspects; Infection; Infections; Methylation; Pathogenesis; Peptides; Peste des petits ruminants; Peste des petits ruminants virus; Physiological aspects; Post-translation; Post-translational modification; Post-translational modification, protein-protein interaction; Protein binding; Protein folding; Protein interaction; Protein-protein interactions; Proteins; Proteomics; Quantitative analysis; Ruminants; Vero cells; Viral infections; Viruses
• ISSN: 1743-422X; 1743-422X
• DOI: 10.1186/s12985-023-02200-1

Peste des petits ruminants virus (PPRV) is a highly contagious pathogen that strongly influences the productivity of small ruminants worldwide. Acetylation is an important post-translational modification involved in regulation of multiple biological functions. However, the extent and function of acetylation in host cells during PPRV infection remains unknown. Dimethylation-labeling-based quantitative proteomic analysis of the acetylome of PPRV-infected Vero cells was performed. In total, 1068 proteins with 2641 modification sites were detected in response to PPRV infection, of which 304 differentially acetylated proteins (DAcPs) with 410 acetylated sites were identified (fold change < 0.83 or > 1.2 and P < 0.05), including 109 up-regulated and 195 down-regulated proteins. Gene Ontology (GO) classification indicated that DAcPs were mostly located in the cytoplasm (43%) and participated in cellular and metabolic processes related to binding and catalytic activity. Functional enrichment indicated that the DAcPs were involved in the minichromosome maintenance complex, unfolded protein binding, helicase activity. Only protein processing in endoplasmic reticulum pathway was enriched. A protein-protein interaction (PPI) network of the identified proteins further indicated that a various chaperone and ribosome processes were modulated by acetylation. To the best of our knowledge, this is the first study on acetylome in PPRV-infected host cell. Our findings establish an important baseline for future study on the roles of acetylation in the host response to PPRV replication and provide novel insights for understanding the molecular pathological mechanism of PPRV infection.