posted on 2016-06-20, 00:00authored byJintao Guo, Changwei Wang, Yi Han, Zhiyong Liu, Tian Wu, Yan Liu, Yang Liu, Yaoju Tan, Xinshan Cai, Yuanyuan Cao, Bangxing Wang, Buchang Zhang, Chunping Liu, Shouyong Tan, Tianyu Zhang
Mycobacterium
abscessus (MAB), which manifests
in the pulmonary system, is one of the neglected causes of nontuberculous
mycobacteria (NTM) infection. Treatment against MAB is difficult,
characterized by its intrinsic antibiotic drug resistance. Lysine
acetylation can alter the physiochemical property of proteins in living
organisms. This study aimed to determine if this protein post-translational
modification (PTM) exists in a clinical isolate M. abscessus GZ002. We used the antiacetyl-lysine immunoprecipitation to enrich
the low-abundant PTM proteins, followed by the LC–MS/MS analysis.
The lysine acetylome of M. abscessus GZ002 was determined.
There were 459 lysine acetylation sites found in 289 acetylated proteins.
Lysine acetylation occurred in 5.87% of the M. abscessus GZ002 proteome, and at least 25% of them were growth essential.
Aerobic respiration and carbohydrate metabolic pathways of M. abscessus GZ002 were enriched with lysine acetylation.
Through bioinformatics analysis, we identified four major acetyl motif
logos (KacY, KacF, KacH, and DKac). Further comparison of the reported M. tuberculosis (MTB) acetylomes and that of MAB GZ002 revealed several common features
between these two species. The lysine residues of several antibiotic-resistance,
virulence, and persistence-related proteins were acetylated in both
MAB GZ002 and MTB. There were 51 identical acetylation sites in 37
proteins found in common between MAB GZ002 and MTB. Overall, we demonstrate
a profile of lysine acetylation in MAB GZ002 proteome that shares
similarities with MTB. Interventions that target at these conserved
sections may be valuable as anti-NTM or anti-TB therapies.