Publikationsdatenbank

Proteome Analysis of an M.avium Mutant Exposes a Novel Role of the Bifunctional Protein LysX in Regulation of Metabolic Activity (2018)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Kirubakar, Greana

Murugaiyan, Jayaseelan (WE 10)

Schaudinn, Christoph

Dematheis, Flavia

Holland, Gudrun

Eravci, Murat

Weise, Christoph

Roesler, Uwe (WE 10)

Lewin, Astrid

Quelle

The Journal of infectious diseases

Bandzählung: 218

Heftzählung: 2

Seiten: 291 – 299

ISSN: 0022-1899

Sprache

Englisch

Verweise

DOI: 10.1093/infdis/jiy100

Pubmed: 29471363

Kontakt

Institut für Tier- und Umwelthygiene

Robert-von-Ostertag-Str. 7-13
14169 Berlin
+49 30 838 51845
tierhygiene@vetmed.fu-berlin.de

Abstract / Zusammenfassung

Lysyl-phosphatidylglycerol (L-PG) is one of the components of the mycobacterial membrane which contributes to the resistance towards cationic antimicrobial peptides, a host-induced frontline defense against invading pathogens. Its production is catalyzed by LysX, a bifunctional protein with lysyl transferase and lysyl-tRNA synthetase activity. Comparative proteome analysis of a lysX mutant of M. avium strain104 and the wild type indicated that the lysX mutant strain undergoes a transition in phenotype by switching the carbon metabolism to β-oxidation of fatty acids along with accumulation of lipid inclusions. Surprisingly, proteins associated with intracellular survival were upregulated in the lysX mutant even during the extracellular growth preparing the bacteria to the conditions occurring inside host cells. In line with this, the lysX mutant exhibited an enhanced intracellular growth in human blood-derived monocytes. Thus, our study exposes the significance of the gene lysX in the metabolism and virulence of the environmental pathogen, M. avium hominissuis.