Differential Abundance of Protein Acylation in Mycobacterium tuberculosis Under Exposure to Nitrosative Stress.

Autor: Birhanu AG; Institute of Biotechnology, Addis Ababa University, Addis Ababa, Ethiopia.; Department of Microbiology, University of Oslo, Nydalen, Oslo, Norway., Riaz T; Department of Microbiology, University of Oslo, Nydalen, Oslo, Norway., Støen M; Department of Microbiology, Oslo University Hospital, Nydalen, Oslo, Norway., Tønjum T; Department of Microbiology, University of Oslo, Nydalen, Oslo, Norway.; Department of Microbiology, Oslo University Hospital, Nydalen, Oslo, Norway.
Jazyk: angličtina
Zdroj: Proteomics. Clinical applications [Proteomics Clin Appl] 2024 Nov; Vol. 18 (6), pp. e202300212. Date of Electronic Publication: 2024 Jul 31.
DOI: 10.1002/prca.202300212
Abstrakt: Background: Human macrophages generate antimicrobial reactive nitrogen species in response to infection by Mycobacterium tuberculosis (Mtb). Exposure to these redox-reactive compounds induces stress response in Mtb, which can affect posttranslational modifications (PTM).
Methods: Here, we present the global analysis of the PTM acylation of Mtb proteins in response to a sublethal dose of nitrosative stress in the form of nitric oxide (NO) using label free quantification.
Results: A total of 6437 acylation events were identified on 1496 Mtb proteins, and O-acylation accounted for 92.2% of the events identified, while 7.8% were N-acylation events. About 22% of the sites identified were found to be acylated by more than one acyl-group. Furthermore, the abundance of each acyl-group decreased as their molecular weight increased. Quantitative PTM analysis revealed differential abundance of acylation in proteins involved in stress response, iron ion homeostasis, growth, energy metabolism, and antimicrobial resistance (AMR) induced by nitrosative stress over time.
Conclusions: The results reveal a potential role of Mtb protein acylation in the bacterial stress responses and AMR. To our knowledge, this is the first report on global O-acylation profile of Mtb in response to NO. This will significantly improve our understanding of the changes in Mtb acylation under nitrosative stress, highly relevant for global health.
(© 2024 The Author(s). PROTEOMICS ‐ Clinical Applications published by Wiley‐VCH GmbH.)
Databáze: MEDLINE
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