Cristin-resultat-ID: 1732764
Sist endret: 1. oktober 2019, 23:18
Resultat
Vitenskapelig foredrag
2019

Abundance of post-translational modifications in Mycobacterium tuberculosis

Bidragsytere:
  • Tone Tonjum
  • Alemayehu Godana Birhanu
  • Tahira Riaz og
  • Solomon Abebe Yimer

Presentasjon

Navn på arrangementet: ECCMID
Sted: Amsterdam
Dato fra: 13. april 2019
Dato til: 16. april 2019

Arrangør:

Arrangørnavn: ESCMID

Om resultatet

Vitenskapelig foredrag
Publiseringsår: 2019

Beskrivelse Beskrivelse

Tittel

Abundance of post-translational modifications in Mycobacterium tuberculosis

Sammendrag

Background Mycobacterium tuberculosis (Mtb) is the causative agent of tuberculosis (TB), one of the top 10 causes of death worldwide and the leading cause of death from infectious disease. Despite the discovery of a multitude of Mtb strains with a high degree of genetic conservation, only a few sub-groups cause extensive outbreaks and antimicrobial drug resistance (AMR), with different clinical presentations in terms of transmissibility, virulence and elicited immune responses. Various regulatory mechanisms contribute to the complexity of the simpler genomes and proteomes of Mtb, and post-translational modifications (PTMs) play a significant role in this variability. PTMs allow bacteria to rapidly alter protein activity in response to host factors and have been implicated in Mtb virulence and AMR. Our aim is to characterize the global acetylome and glycoproteomic profile of different Mtb lineages, to unveil the role of these PTMs in mycobacterial adaptation, survival and AMR. Materials/methods The global acetylome and glycoproteomic patterns in five Mtb strains, four clinical isolates including the slow-growing lineage 7 and the reference strain H37Rv, were analyzed. Mtb cell lysates were subjected to in-gel trypsin digestion and injected into a Nano LC-MS/MS mass spectrometer (Thermo Scientific). The MaxQuant and Perseus softwares were used peptide search and PTM site identification. Poteins were searched for 57 different glycan residues. The findings on N-linked protein glycosylation were verified by manual inspection. The Cytoscape plug-in MCODE was used to develop protein-protein interaction networks. Results Our analysis resulted in the identification of 2944 glycosylation sites on 1325 proteins and 2490 acetylation sites on 953 proteins. Notably, we report 489 sites that were N-glycosylated at N residues (17% of the total glycosylation events). The study identified strain-specific qualitative and quantitative differences in PTM abundances on proteins involved in virulence, pathogenesis and AMR. Conclusions Notably, this study reports a vast abundance of PTMs in clinical Mtb strains and is the first report on N-linked glycosylation and O-acetylation in Mtb. These novel PTM data also explain the role of protein acetylation and glycosylation in creating phenotypic variability and fitness for survival among the genetically conserved lineages of Mtb.

Bidragsytere

Tone Tønjum

Bidragsyterens navn vises på dette resultatet som Tone Tonjum
  • Tilknyttet:
    Forfatter
    ved Avdeling for mikrobiologi ved Oslo universitetssykehus HF
  • Tilknyttet:
    Forfatter
    ved Avdeling for mikrobiologi ved Universitetet i Oslo

Alemayehu Godana Birhanu

  • Tilknyttet:
    Forfatter
    ved Avdeling for mikrobiologi ved Universitetet i Oslo

Tahira Riaz

  • Tilknyttet:
    Forfatter
    ved Avdeling for mikrobiologi ved Universitetet i Oslo

Solomon Abebe Yimer

  • Tilknyttet:
    Forfatter
1 - 4 av 4