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mutans, indicating that the modification of cell membrane structure, redistribution of energy metabolism and enhanced nucleic acid machinery contributed to the S. We identified distinct variations and diverse modulators caused by murI mutation in the proteome of S. The DEPs significantly upregulated after murI knockout had roles in diverse functional processes spanning cell-wall biosynthesis, energy production, and DNA replication and repair. PPI analysis revealed a complex network of DEPs containing 191 edges and 122 nodes. The ΔmurI cells displayed an increase in the relative expression of 93 proteins (fold change ≥ 1.2, p < 0.05) and a decrease in 29 proteins (fold change ≤ 0.833, p < 0.05) compared with the wild-type cells. mutans UA159 with or without the murI mutation. Among 1173 total bacterial proteins identified, 112 DEPs exhibited altered expression patterns in S.
Finally, a protein–protein interaction (PPI) network was established using the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING). Furthermore, differentially expressed proteins (DEPs) were identified by Mascot, Gene Ontology (GO) annotation, Cluster of Orthologous Groups of proteins (COG), and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analyses. mutans FW1718 and UA159 were assessed by iTRAQ-coupled LC–ESI–MS/MS. the wild-type strain in chemically defined media to elucidate the mechanisms by which S. In this study, we applied isobaric tags for relative and absolute quantitation (iTRAQ)-based proteomics to characterize the proteome profiles of the murI mutant strain vs. mutans FW1718), with the hereditary background of UA159, displayed alterations of morphogenesis, attenuated stress tolerance, and weakened biofilm-forming capabilities, accompanying with unclear mechanisms. Our previous study noted that a glutamate racemase (MurI) mutant strain (designated S. Streptococcus mutans UA159 is responsible for human dental caries with robust cariogenic potential.
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