Identification and Quantification of S-Sulfenylation Proteome of Mycobacterium tuberculosis under Oxidative Stress

• DOI: 10.1128/spectrum.03386-22
• Publication Date: 2023-03-21T14:05:48Z
• Authors: Yun Lu; Hongtong Chen; Penghe Wang; Jing Pang; Xi Lu; Guoqing Li; Xinxin Hu; Xiukun Wang; Xinyi Yang; Congran Li; Yu Lu; Xuefu You
• Keywords: Proteome; Identification

The ability to maintain redox homeostasis is critical for Mycobacterium tuberculosis (Mtb) survive the stress of host. There are many antioxidant systems in Mtb ensure its normal replication and survival host, cysteine thiols one them. S-sulfenylation reversible modifications resist oxidative stress. In study, we investigated total modification proteome under provided by hydrogen peroxide. To determine quantify modified proteins, high specific IodoTMT6plex reagents resolution mass spectrometry were used label peptides proteins modified. significant differences levels 279 297 peroxide Functional enrichment analysis indicated that these cysteine-modified involved oxidation-reduction process, fatty acid biosynthetic response, protein repair, cell wall, etc. conclusion, our study provides a view stress, revealing series may play role maintaining homeostasis. IMPORTANCE With continuous spread drug-resistant tuberculosis, there an urgent need new antituberculosis drugs with mechanisms. extremely important residues have dual protection from irreversible damage functions regulation, which plays system. Thus, discover changes level quintessential elucidate mechanism. Our results list process potentially could be considered targets drug discovery vaccine development. Furthermore, it first S-sulfenylation-modified Mtb, better insight into response host defense enable deeper understanding strategies.