Ser/Thr/Tyr phosphoproteome characterization of Acinetobacter baumannii: Comparison between a reference strain and a highly invasive multidrug-resistant clinical isolate
In: Journal of Proteomics, Jg. 102 (2014-05-01), S. 113-124
Online
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Zugriff:
In the current study, the Ser/Thr/Tyr phosphoproteomes of two Acinetobacter baumannii strains, reference (ATCC17978) and highly invasive multidrug-resistant clinical isolate (Abh12O-A2) were analyzed using SCX and TiO 2 chromatography followed by high resolution mass spectrometry. We detected a total of 201 unique phosphorylation sites (p-sites), and, after manual validation of peptide spectra, 91 high-confidence phosphorylation events (p-events) could be localized to a specific amino acid residue. The percentage distribution of Ser/Thr/Tyr phosphorylation was 68.9% on serine, 24.1% on threonine and 5.2% on tyrosine in ATCC17978, and 70.8% on serine, 25.2% on threonine and 3.8% on tyrosine in AbH12O-A2. Across all identified p-sites, 11 were identified in ATCC17978 only, while 43 were identified in Abh12O-A2 only, and 37 overlapped between the two strains. Here for the first time we describe the phosphoproteome of A. baumanii , and significance of selected phosphorylation sites is discussed in the context of stress/starvation, pathogenicity and drug resistance. Biological significance It is now well established that protein phosphorylation on Ser/Thr/Tyr residues is an important post-translational modification in bacteria. Herein we employed SCX and TiO 2 chromatographic phosphopeptide enrichment combined with LTQ-Orbitrap mass spectrometric analyses to characterize and establish a qualitative comparison between the Ser/Thr/Tyr phosphoproteomes of two Acinetobacter baumannii strains: a reference strain and a highly invasive multidrug-resistant clinical isolate. We highlight the identification of phosphoproteins with a role in pathogenicity and those involved in drug resistance.
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Ser/Thr/Tyr phosphoproteome characterization of Acinetobacter baumannii: Comparison between a reference strain and a highly invasive multidrug-resistant clinical isolate
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Autor/in / Beteiligte Person: | Aranda, Jesús ; Nakedi, Kehilwe C. ; Spät, Philipp ; Soares, Nelson C. ; Jose Antonio Mendez ; Bou, Germán |
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Zeitschrift: | Journal of Proteomics, Jg. 102 (2014-05-01), S. 113-124 |
Veröffentlichung: | Elsevier BV, 2014 |
Medientyp: | unknown |
ISSN: | 1874-3919 (print) |
DOI: | 10.1016/j.jprot.2014.03.009 |
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