Proteomics and metabolomics analyses of Streptococcus agalactiae isolates from human and animal sources

Abstract

Streptococcus agalactiae (S. agalactiae), group B Streptococcus (GBS), a major cause of infection in a wide variety of diseases, have been compared in different human and animal sources. We aimed to compare the bacterial proteome and metabolome profiles of human and animal S. agalactiae strains to delineate biological interactions relevant to infection. With the innovative advancement in mass spectrometry, a comparative result between both strains provided a solid impression of different responses to the host. For instance, stress-related proteins (Asp23/Gls24 family envelope stress response protein and heat shock protein 70), which play a role in the survival of GBS under extreme environmental conditions or during treatment, are highly expressed in human and animal strains. One human strain contains ꞵ-lactamase (serine hydrolase) and biofilm regulatory protein (lytR), which are important virulence regulators and potential targets for the design of novel antimicrobials. Another human strain contains the aminoglycosides-resistance bifunctional AAC/APH (A0A0U2QMQ5) protein, which confers resistance to almost all clinically used aminoglycosides. Fifteen different metabolites were annotated between the two groups. L-aspartic acid, ureidopropionic acid, adenosine monophosphate, L-tryptophan, and guanosine monophosphate were annotated at higher levels in human strains. Butyric acid, fumaric acid, isoleucine, leucine, and hippuric acid have been found in both human and animal strains. Certain metabolites were uniquely expressed in animal strains, with fold changes greater than 2. For example, putrescine modulates biofilm formation. Overall, this study provides biological insights into the substantial possible bacterial response reflected in its macromolecular production, either at the proteomic or metabolomic level.

An Explainable Deep Learning Classifier of Bovine Mastitis Based on Whole-Genome Sequence Data—Circumventing the p >> n Problem

“…Furthermore, due to the ATP substrate mentioned above and its specific channels, alterations in the number of molecules that activate these channels influence their activity (GO:0022838), causing, in the case of bovine mastitis, an increase in the inflammatory response, which also indicates the role of GTP binding in the immune response to bovine mastitis, and which overlaps with our findings of the significant molecular functions of small GTPases binding (GO:0031267) and the activity of the GTPase activator (GO:0005096). Furthermore, GTPase-regulated pathways have often been mentioned in the context of mastitis, especially with respect to inflammation caused by Streptococcus agalactiae and Mycoplasma bovis [35][36][37][38][39][40]. Inflammation, which is the consequence of infection, involves exocytosis that leads to the release of granule/vesicle contents to the cell exterior.…”