iProXProteomicsXiangmin LinEdwardsiella Tarda Eib202http://www.iprox.org/page/project.html?id=IPX0004440000313461278@qq.comFujian Agriculture and Forestry UniversityiProXThe antibiotic resistance of <i>Edwardsiella tarda</i> is becoming increasingly prevalent, and thus novel antimicrobial strategies are being sought. Lysine acylation has been demonstrated to play an important role in bacterial physiological functions, while its role in bacterial antibiotic resistance remains largely unclear. In this study, we investigated the lysine acetylation and succinylation profiles of <i>E. tarda</i> strain EIB202 using affinity antibody purification combined with LC-MS/MS. A total of 1511 lysine-acetylation sites were identified on 589 proteins, and 2346 lysine-succinylation sites were further identified on 692 proteins of this pathogen. Further bioinformatic analysis showed that both post-translational modifications (PTMs) were enriched in the tricarboxylic acid (TCA) cycle, pyruvate metabolism, biosynthesis, and carbon metabolism. In addition, 948 peptides of 437 proteins had overlapping associations with multiple metabolic pathways. Moreover, both acetylation and succinylation were found in many antimicrobial resistance (AMR) proteins, suggesting their potentially vital roles in antibiotic resistance. In general, our work provides insights into the acetylome and succinylome features responsible for the antibiotic resistance mechanism of <i>E. tarda</i>, and the results may facilitate future investigations into the pathogenesis of this bacterium.Acetylome and Succinylome Profiling of <i>Edwardsiella tarda</i> Reveals Key Roles of Both Lysine Acylations in Bacterial Antibiotic Resistance.Fu Yuying Y, Zhang Lishan L, Song Huanhuan H, Liao Junyan J, Lin Li L, Jiang Wenjia W, Wu Xiaoyun X, Wang Guibin GfalseEdwardsiella tarda strain EIB 202 lysine acetylation and succinylationThe antibiotics resistance of Edwardsiella tarda is prevailing, seeking a novel antimicrobial strategies extremely urgent. Lysine acylation has been proved to play important role on the bacterial physiological function while its role on bacterial antibiotics resistance mechanism still largely unclear. In this study, we investigated the lysine acetylation and succinylation profiles of E. tarda stain EIB202 using affinity antibody purification combined with LC MS/MS. A total of 1511 lysine-acetylation sites were identified on 589 proteins, and 2346 lysine-succinylation sites were further identified on 692 proteins of this pathogen. Further bioinformatics analysis showed that both PTMs prefer to enrich in TCA cycle, pyruvate metabolism. biosynthesis, and carbon metabolism. Besides, 948 peptides of 437 proteins were found to be overlap and associated with multiple metabolic pathways. Moreover, both the acetylation and succinylation were found in many antimicrobial resistance (AMR) proteins, suggesting its potentially vital role in antibiotic resistance. In general, our work provides insights into the acetylome and succinylome features responsible for the antibiotic resistance mechanism of E. tarda, which may facilitate future investigations on the pathogenesis of this bacterium.Thu May 12 00:00:00 BST 2022PXD03381849821735884095