title: Proteomic characterization of Nα- and Nε-acetylation in Acinetobacter baumannii.
abstract: Nα- and Nε-acetylation represent a pivotal post-translational modification used by both eukaryotes and prokaryotes to modulate diverse biological processes. Acinetobacter baumannii has been described as an important nosocomial pathogen for the past 30 years, frequently involved in ventilator-associated pneumonia, bloodstream and urinary tract infections. Many aspects of the biology of A. baumannii remain elusive, in particular the extent and function of N-acetylation. We investigated here N-acetylation in A. baumannii strain ATCC 17978 by proteomic analysis, and we showed the usefulness of using different analytical approaches. Overall, we identified 525 N-acetylated proteins in which, 145 were Nα-acetylated and 411 were Nε-acetylated. Among them, 41 proteins carried both types of N-acetylation. We found that N-acetylation may play a role in biofilm formation, bacterial virulence (e.g. in several iron acquisition pathways), as well as a number of phenotypes, such as, stress adaptation and drug resistance.
  
  
  
  This study is the first to perform the N-acetylome of A. baumannii using different analytical approaches. Each analytical tool permitted to characterize distinctive modified peptides. The combination of all these methods allowed us to identify 145 and 411 Nα- and Nε-acetylated proteins. Besides the fact that acetylation was involved in central metabolism as previously described in other bacteria, some N-acetylated proteins showed interesting role in bacterial virulence (iron acquisition), biofilm formation, stress adaptation and drug resistance of A. baumannii.
authors.affiliation: CNRS, UMR 6270, Polymères, Biopolymères, Surfaces Laboratory, F-76821 Mont-Saint-Aignan, France; Normandie Univ, UR, France.
authors.forename: Takfarinas
authors.initials: T
authors.lastname: Kentache
authors.affiliation: CNRS, UMR 6270, Polymères, Biopolymères, Surfaces Laboratory, F-76821 Mont-Saint-Aignan, France; Normandie Univ, UR, France; PISSARO proteomic facility, IRIB, F-76821 Mont-Saint-Aignan, France.
authors.forename: Thierry
authors.initials: T
authors.lastname: Jouenne
authors.affiliation: CNRS, UMR 6270, Polymères, Biopolymères, Surfaces Laboratory, F-76821 Mont-Saint-Aignan, France; Normandie Univ, UR, France; PISSARO proteomic facility, IRIB, F-76821 Mont-Saint-Aignan, France.
authors.forename: Emmanuelle
authors.initials: E
authors.lastname: Dé
authors.affiliation: CNRS, UMR 6270, Polymères, Biopolymères, Surfaces Laboratory, F-76821 Mont-Saint-Aignan, France; Normandie Univ, UR, France; PISSARO proteomic facility, IRIB, F-76821 Mont-Saint-Aignan, France. Electronic address: julie.hardouin@univ-rouen.fr.
authors.forename: Julie
authors.initials: J
authors.lastname: Hardouin
mesh_terms: D000107:Acetylation; D040981:Acinetobacter baumannii / Q000378:metabolism*; D000222:Adaptation, Physiological; D001426:Bacterial Proteins / Q000378:metabolism*; D018441:Biofilms / Q000254:growth & development; D004351:Drug Resistance; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D040901:Proteomics / Q000379:methods*; D014774:Virulence
chemical_list: D001426:Bacterial Proteins
keywords: Acinetobacter baumannii; Lysine acetylation; N-terminal acetylation; Proteomics