In silico Analysis of the Stability of Ribosomal Protein S1 from Various Strains of the Pathogenic Microorganism Staphylococcus aureus.
The pathogenic microorganism Staphylococcus aureus , one of the representatives of the staphylococcus family, is capable of developing resistance to antibiotics and antiseptics. The largest ribosomal protein, S1, from S. aureus contains four structural S1 domains, and short peptides synthesized based on its sequence have amyloidogenic and antimicrobial properties (antimicrobial peptides). In this work, in silico analysis of all available ribosomal protein S1 sequences from various S. aureus strains allowed us to identify residues that are characteristic of specific strains. Based on data from the I-Mutant service, changes in the stability of ribosomal protein S1 from various S. aureus strains were predicted. The results obtained will be used in the future for targeted mutations in the design of new antimicrobial peptides based on ribosomal protein S1.
Authors
- Oxana V. Galzitskaya (ORCID: https://orcid.org/0000-0002-3962-1520)
- Andrey V. Machulin (ORCID: https://orcid.org/0000-0002-4859-7219)
- Evgenia I. Deryusheva (ORCID: https://orcid.org/0000-0002-6213-2784)
Institutions
- Institute of Theoretical and Experimental Biophysics (RU)
- Institute for Biological Instrumentation (RU)
- Institute of Protein Research (RU)
- G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms (RU)
- Pushchino Scientific Center for Biological Research
Publication Details
- Journal
- Journal Biomed
- Published
- 2024-11-06
- DOI
- https://doi.org/10.33647/2074-5982-20-3-32-36
- Primary Topic
- Antimicrobial Peptides and Activities
- Type
- article
- Field-Weighted Citation Impact
- 0.00