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A Fluorescence-based Method to Study Bacterial Gene Regulation in Infected Tissues
Published on: February 19, 2019
A peptide factor secreted by Staphylococcus pseudintermedius exhibits properties of both bacteriocins and virulence
Benedykt Wladyka1,2, Marcin Piejko1,3, Monika Bzowska4,2
1Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Krakow, Poland.
Abstract:
Staphylococcus pseudintermedius is a common commensal bacterium colonizing the skin and mucosal surfaces of household animals. However, it has recently emerged as a dangerous opportunistic pathogen, comparable to S. aureus for humans. The epidemiological situation is further complicated by the increasing number of methicillin-resistant S. pseudintermedius infections and evidence of gene transmission driving antibiotic resistance between staphylococci colonizing human and zoonotic hosts. In the present study, we describe a unique peptide, BacSp222, that possesses features characteristic of both bacteriocins and virulence factors. BacSp222 is secreted in high quantities by S. pseudintermedius strain 222 isolated from dog skin lesions. This linear, fifty-amino-acid highly cationic peptide is plasmid-encoded and does not exhibit significant sequence similarities to any other known peptides or proteins. BacSp222 kills gram-positive bacteria (at doses ranging from 0.1 to several micromol/l) but also demonstrates significant cytotoxic activities towards eukaryotic cells at slightly higher concentrations. Moreover, at nanomolar concentrations, the peptide also possesses modulatory properties, efficiently enhancing interferon gamma-induced nitric oxide release in murine macrophage-like cell lines. BacSp222 appears to be one of the first examples of multifunctional peptides that breaks the convention of splitting bacteriocins and virulence factors into two unrelated groups.
Insights
Researchers discovered BacSp222, a unique peptide from Staphylococcus pseudintermedius. This multifunctional peptide acts as both a bacteriocin and a virulence factor, impacting bacterial and eukaryotic cells.
Area of Science:
- Microbiology
- Molecular Biology
- Immunology
Background:
- Staphylococcus pseudintermedius is an opportunistic pathogen in animals, with rising methicillin-resistant strains.
- Gene transmission of antibiotic resistance between human and animal staphylococci is a growing concern.
- Bacteriocins and virulence factors are typically considered distinct categories of microbial molecules.
Purpose of the Study:
- To characterize a novel peptide, BacSp222, secreted by Staphylococcus pseudintermedius.
- To investigate the dual functionality of BacSp222 as a potential bacteriocin and virulence factor.
Main Methods:
- Isolation and characterization of the BacSp222 peptide from S. pseudintermedius strain 222.
- Determination of peptide sequence, physicochemical properties, and genetic origin (plasmid-encoded).
- Assessment of antimicrobial activity against Gram-positive bacteria and cytotoxicity against eukaryotic cells.
- Evaluation of immunomodulatory effects on macrophage nitric oxide production.
Main Results:
- BacSp222 is a novel, linear, 50-amino acid, highly cationic peptide with no significant sequence homology to known proteins.
- The peptide exhibits potent bactericidal activity against Gram-positive bacteria at micromolar concentrations.
- BacSp222 demonstrates cytotoxicity towards eukaryotic cells at slightly higher concentrations.
- At nanomolar concentrations, BacSp222 enhances interferon gamma-induced nitric oxide release in murine macrophages.
Conclusions:
- BacSp222 represents a unique multifunctional peptide with both antimicrobial and immunomodulatory properties.
- This finding challenges the traditional separation of bacteriocins and virulence factors.
- BacSp222 offers a potential new avenue for understanding host-pathogen interactions and developing novel therapeutic strategies.
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