1. Transcriptional Analysis and Identification of a Peptidoglycan Hydrolase (PGH) and a Ribosomal Protein with Antimicrobial Activity Produced by Lactiplantibacillus paraplantarum .
- Author
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Hurtado-Rios JJ, Carrasco-Navarro U, Almanza-Pérez JC, Rincón-Guevara MA, and Ponce-Alquicira E
- Subjects
- N-Acetylmuramoyl-L-alanine Amidase metabolism, N-Acetylmuramoyl-L-alanine Amidase genetics, Bacterial Proteins metabolism, Bacterial Proteins genetics, Anti-Bacterial Agents pharmacology, Microbial Sensitivity Tests, Anti-Infective Agents pharmacology, Gene Expression Regulation, Bacterial drug effects, Ribosomal Proteins metabolism, Ribosomal Proteins genetics
- Abstract
The growing challenge of antibiotic resistance has intensified the search for new antimicrobial agents. Promising alternatives include peptidoglycan hydrolases (PGHs) and certain ribosomal proteins, both of which exhibit antimicrobial activity. This study focuses on a Lactiplantibacillus paraplantarum strain, isolated from fermented meat, capable of inhibiting pathogens such as Listeria innocua , Salmonella Typhimurium , Escherichia coli , Staphylococcus aureus , and Weissella viridescens . The highest growth and antimicrobial activity were observed at a high nitrogen concentration (5.7 g/L). Two antimicrobial proteins were identified: the 50S ribosomal protein L14 (RP uL14) and 6-phospho- N -acetylmuramidase (MupG), a PGH. Partial purification and characterization of these proteins were achieved using SDS-PAGE, zymography, and LC-MS/MS. Transcriptional data (RT-qPCR) showed that higher nitrogen concentrations enhanced MupG expression, while increased carbon concentrations boosted RP uL14 expression. These findings highlight the importance of nutritional sources in maximizing the production of novel antimicrobial proteins, offering a potential path to develop effective alternatives against antibiotic-resistant bacteria.
- Published
- 2024
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