Abstract
Bacterial effector molecules are crucial infectious agents that can cause pathogenesis. In the present study, the pathogenesis of toxic Salmonella enterica serovar Typhi (S. Typhi) proteins on the model host Caenorhabditis elegans was investigated by exploring the host's regulatory proteins during infection through the quantitative proteomics approach. Extracted host proteins were analyzed using two-dimensional gel electrophoresis (2D-GE) and differentially regulated proteins were identified using MALDI TOF/TOF/MS analysis. Of the 150 regulated proteins identified, 95 were downregulated while 55 were upregulated. The interaction network of regulated proteins was predicted using the STRING tool. Most downregulated proteins were involved in muscle contraction, locomotion, energy hydrolysis, lipid synthesis, serine/threonine kinase activity, oxidoreductase activity, and protein unfolding. Upregulated proteins were involved in oxidative stress pathways. Hence, cellular stress generated by S. Typhi proteins in the model host was determined using lipid peroxidation as well as oxidant and antioxidant assays. In addition, candidate proteins identified via extract analysis were validated by western blotting, and the roles of several crucial molecules were analyzed in vivo using transgenic strains (myo-2 and col-19) and mutant (ogt-1) of C. elegans. To the best of our knowledge, this is the first study to report protein regulation in host C. elegans exposed to toxic S. Typhi proteins. It highlights the significance of p38 MAPK and JNK immune pathways.
Highlights
Bacterial effector molecules are the crucial infectious agents and are sufficient to cause pathogenesis
Each experiment was performed in biological triplicates and the error bars represent the mean ± SD (*p < 0.05)
The result clearly denoted that there was no significant (p < 0.05) difference between mean life span in overnight digested protein fractions and control worms fed with E. coli OP50 which suggested that only the protein fractions have modulated the C. elegans lifespan and morphology (Fig. 1B)
Summary
Bacterial effector molecules are the crucial infectious agents and are sufficient to cause pathogenesis. Typhi) toxic proteins on the model host Caenorhabditis elegans was investigated by exploring the host regulatory proteins during infection through quantitative proteomics approach. In this regard, the host protein extract was analysed using two-dimensional gel electrophoresis (2D-GE) and differentially regulated proteins were identified using MALDI TOF/TOF/MS analysis.Results: Out of the 150 regulated proteins identified, 95 proteins were appeared to be downregulated while 55 were upregulated. Typhi protein extract on the model host was determined using lipid peroxidation, oxidant and antioxidant assays. C. elegans is a well suited model to investigate the cellular impact of bacterial toxic proteins since the model has been well established for its utility in toxicological studies. It was reported that the lipoteichoic acid of Gram-positive bacteria is equivalently antigenic to LPS which elicit the inflammatory response in the host (JebaMercy et al, 2015)
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