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Updated: Apr 12, 2026

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Time dynamics of the Bacillus cereus exoproteome are shaped by cellular oxidation
Jean-Paul Madeira1, Béatrice Alpha-Bazin2, Jean Armengaud2
1UMR408, Sécurité et Qualité des Produits d'Origine Végétale, Université d'Avignon Avignon, France ; INRA, UMR408, Sécurité et Qualité des Produits d' Origine Végétale Avignon, France ; Commissariat à l'énergie Atomique et aux Énergies Alternatives (CEA), Direction des Sciences du Vivant (DSV), IBEB, Li2D Bagnols sur Cèze, France.
Abstract:
At low density, Bacillus cereus cells release a large variety of proteins into the extracellular medium when cultivated in pH-regulated, glucose-containing minimal medium, either in the presence or absence of oxygen. The majority of these exoproteins are putative virulence factors, including toxin-related proteins. Here, B. cereus exoproteome time courses were monitored by nanoLC-MS/MS under low-oxidoreduction potential (ORP) anaerobiosis, high-ORP anaerobiosis, and aerobiosis, with a specific focus on oxidative-induced post-translational modifications of methionine residues. Principal component analysis (PCA) of the exoproteome dynamics indicated that toxin-related proteins were the most representative of the exoproteome changes, both in terms of protein abundance and their methionine sulfoxide (Met(O)) content. PCA also revealed an interesting interconnection between toxin-, metabolism-, and oxidative stress-related proteins, suggesting that the abundance level of toxin-related proteins, and their Met(O) content in the B. cereus exoproteome, reflected the cellular oxidation under both aerobiosis and anaerobiosis.
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