INTRAVENOUS IMMUNOGLOBULIN INDUCES ANERGY STATELIKE OF AUTO-REACTIVE B LYMPHOCYTES IN SJÖGREN’S SYNDROME

Oral Communication presented at the ";Forum des Jeunes Chercheurs";, Brest (France) 2011

Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress.

Hillion M, Bernhardt J, Busche T, et al. Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress. Sci Rep. 2017;7(1): 1195.Mycothiol (MSH) is the major low molecular weight (LMW) thiol in Actinomycetes. Here, we used shotgun proteomics, OxICAT and RNA-seq transcriptomics to analyse protein S-mycothiolation, reversible thiol-oxidations and their impact on gene expression in Mycobacterium smegmatis under hypochlorite stress. In total, 58 S-mycothiolated proteins were identified under NaOCl stress that are involved in energy metabolism, fatty acid and mycolic acid biosynthesis, protein translation, redox regulation and detoxification. Protein S-mycothiolation was accompanied by MSH depletion in the thiol-metabolome. Quantification of the redox state of 1098 Cys residues using OxICAT revealed that 381 Cys residues (33.6%) showed >10% increased oxidations under NaOCl stress, which overlapped with 40 S-mycothiolated Cys-peptides. The absence of MSH resulted in a higher basal oxidation level of 338 Cys residues (41.1%). The RseA and RshA anti-sigma factors and the Zur and NrdR repressors were identified as NaOCl-sensitive proteins and their oxidation resulted in an up-regulation of the SigH, SigE, Zur and NrdR regulons in the RNA-seq transcriptome. In conclusion, we show here that NaOCl stress causes widespread thiol-oxidation including protein S-mycothiolation resulting in induction of antioxidant defense mechanisms in M. smegmatis. Our results further reveal that MSH is important to maintain the reduced state of protein thiols

In-depth characterization of CD24(high)CD38(high) transitional human B cells reveals different regulatory profiles

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Superluminal X-shaped beams propagating without distortion along a coaxial guide

In a previous paper [Phys. Rev. E64 (2001) 066603; e-print physics/0001039], we showed that localized Superluminal solutions to the Maxwell equations exist, which propagate down (non-evanescence) regions of a metallic cylindrical waveguide. In this paper we construct analogous non-dispersive waves propagating along coaxial cables. Such new solutions, in general, consist in trains of (undistorted) Superluminal "X-shaped" pulses. Particular attention is paid to the construction of finite total energy solutions. Any results of this kind may find application in the other fields in which an essential role is played by a wave-equation (like acoustics, geophysics, etc.). [PACS nos.: 03.50.De; 41.20;Jb; 83.50.Vr; 62.30.+d; 43.60.+d; 91.30.Fn; 04.30.Nk; 42.25.Bs; 46.40.Cd; 52.35.Lv. Keywords: Wave equations; Wave propagation; Localized beams; Superluminal waves; Coaxial cables; Bidirectional decomposition; Bessel beams; X-shaped waves; Maxwell equations; Microwaves; Optics; Special relativity; Coaxial metallic waveguides; Acoustics; Seismology; Mechanical waves; Elastic waves; Guided gravitational waves.]Comment: plain LaTeX file (22 pages), plus 15 figures; in press in Phys. Rev.

Protein S-Bacillithiolation Functions in Thiol Protection and Redox Regulation of the Glyceraldehyde-3-Phosphate Dehydrogenase Gap in Staphylococcus aureus Under Hypochlorite Stress

Aims: Bacillithiol (BSH) is the major low-molecular-weight thiol of the human pathogen Staphylococcus aureus. In this study, we used OxICAT and Voronoi redox treemaps to quantify hypochlorite-sensitive protein thiols in S. aureus USA300 and analyzed the role of BSH in protein S-bacillithiolation.  Results: The OxICAT analyses enabled the quantification of 228 Cys residues in the redox proteome of S. aureus USA300. Hypochlorite stress resulted in >10% increased oxidation of 58 Cys residues (25.4%) in the thiol redox proteome. Among the highly oxidized sodium hypochlorite (NaOCl)-sensitive proteins are five S-bacillithiolated proteins (Gap, AldA, GuaB, RpmJ, and PpaC). The glyceraldehyde-3-phosphate (G3P) dehydrogenase Gap represents the most abundant S-bacillithiolated protein contributing 4% to the total Cys proteome. The active site Cys151 of Gap was very sensitive to overoxidation and irreversible inactivation by hydrogen peroxide (H2O2) or NaOCl in vitro. Treatment with H2O2 or NaOCl in the presence of BSH resulted in reversible Gap inactivation due to S-bacillithiolation, which could be regenerated by the bacilliredoxin Brx (SAUSA300_1321) in vitro. Molecular docking was used to model the S-bacillithiolated Gap active site, suggesting that formation of the BSH mixed disulfide does not require major structural changes.  Conclusion and Innovation: Using OxICAT analyses, we identified 58 novel NaOCl-sensitive proteins in the pathogen S. aureus that could play protective roles against the host immune defense and include the glycolytic Gap as major target for S-bacillithiolation. S-bacillithiolation of Gap did not require structural changes, but efficiently functions in redox regulation and protection of the active site against irreversible overoxidation in S. aureus. Antioxid. Redox Signal. 28, 410–430