Details

Autor(en) / Beteiligte

• Chandra, Hari Balaji
• Lalhmangaihzuali, L.
• Shome, Arijit
• Sahoo, Raj
• Irungbam, Karuna
• Mahawar, Manish

Titel

Comparative analysis reveals the trivial role of MsrP in defending oxidative stress and virulence of Salmonella Typhimurium in mice

Ist Teil von

• Free radical biology & medicine, 2024-03, Vol.213, p.322-326

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2024

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• Sulphur containing amino acids, methionine and cysteine are highly prone to oxidation. Reduction of oxidized methionine (Met-SO) residues to methionine (Met) by methionine sulfoxide reductases (Msrs) enhances the survival of bacterial pathogens under oxidative stress conditions. S. Typhimurium encodes two types (cytoplasmic and periplasmic) of Msrs. Periplasmic proteins, due to their location are highly vulnerable to host-generated oxidants. Therefore, the periplasmic Msr (MsrP) mediated repair (as compared to the cytoplasmic counterpart) might play a more imperative role in defending host-generated oxidants. Contrary to this, we show that in comparison to the ΔmsrP strain, the mutant strains in the cytoplasmic Msrs (ΔmsrA and ΔmsrAC strains) showed many folds more susceptibility to chloramine-T and neutrophils. Further ΔmsrA and ΔmsrAC strains accumulated higher levels of ROS and showed compromised fitness in mice spleen and liver. Our data suggest the pivotal role of cytoplasmic Msrs in oxidative stress survival of S. Typhimurium. [Display omitted] •Methionine sulfoxide reductases repair oxidized methionine residues, thus aid in survival of the bacterial pathogens.•Compared to ΔmsrP mutant, ΔmsrA and ΔmsrAC mutants show increased sensitivity to chloramine-T and neutrophils.•ΔmsrA and ΔmsrAC strains showed defective fitness in mice.