New antibacterial agents are urgently needed for the elimination of biofilm-forming bacteria that are highly resistant to traditional antimicrobial agents. Proliferation of such bacteria can lead to significant economic losses in the agri-food sector. This study demonstrates the potential of the bacteriophage-derived peptidase, CHAP(K), as a biocidal agent for the rapid disruption of biofilm-forming staphylococci, commonly associated with bovine mastitis. Purified CHAP(K) applied to biofilms of Staphylococcus aureus DPC5246 completely eliminated the staphylococcal biofilms within 4 h. In addition, CHAP(K) was able to prevent biofilm formation by this strain. The CHAP(K) lysin also reduced S. aureus in a skin decolonization model. Our data demonstrates the potential of CHAP(K) as a biocidal agent for prevention and treatment of biofilm-associated staphylococcal infections or as a decontaminating agent in the food and healthcare sectors.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3574654 | PMC |
http://dx.doi.org/10.1155/2013/625341 | DOI Listing |
ACS Appl Bio Mater
November 2024
Institute of Information and Communication Technologies, Electronics and Applied Mathematics, UCLouvain, Place du Levant 1, 1348 Louvain-la-Neuve, Belgium.
Rapid and precise diagnostic techniques are essential for identifying foodborne pathogens, including (), which poses significant challenges to food safety. Traditional detection methods are limited by long incubation times and high costs. In this context, gold nanoparticle (AuNP)-based lateral flow assays (LFAs) are emerging as valuable tools for rapid screening.
View Article and Find Full Text PDFSci Rep
August 2024
Department of Biomedical Science, Acharya Narendra Dev College, University of Delhi, Govindpuri, Kalkaji, New Delhi, 110019, India.
The escalating antibiotic resistance in mycobacterial species poses a significant threat globally, necessitating an urgent need to find alternative solutions. Bacteriophage-derived endolysins, which facilitate phage progeny release by attacking bacterial cell walls, present promising antibacterial candidates due to their rapid lytic action, high specificity and low risk of resistance development. In mycobacteria, owing to the complex, hydrophobic cell wall, mycobacteriophages usually synthesize two endolysins: LysinA, which hydrolyzes peptidoglycan; LysinB, which delinks mycolic acid-containing outer membrane and arabinogalactan, releasing free mycolic acid.
View Article and Find Full Text PDFAppl Microbiol Biotechnol
June 2024
National Veterinary Research Institute, Puławy, 24-100, Poland.
This review gathers all, to the best of our current knowledge, known lysins, mainly bacteriophage-derived, that have demonstrated activity against Bacillus anthracis strains. B. anthracis is a spore-forming, toxin-producing bacteria, naturally dwelling in soil.
View Article and Find Full Text PDFInt J Antimicrob Agents
August 2024
Department of Molecular Science and Technology, Ajou University, Suwon, South Korea; Department of Applied Chemistry and Biological Engineering, Ajou University, Suwon, South Korea. Electronic address:
Objectives: Clostridioides difficile has emerged as a major cause of life-threatening diarrheal disease. Conventional antibiotics used in current standards of care exacerbate the emergence of antibiotic-resistant strains and pose a risk of recurrent C. difficile infection (CDI).
View Article and Find Full Text PDFInt J Antimicrob Agents
August 2024
Department of Integrative Biotechnology, Sungkyunkwan University College of Biotechnology and Bioengineering, Suwon, Republic of Korea; Research Center, MVRIX, Anyang, Republic of Korea. Electronic address:
The emergence of multidrug-resistant pathogens has outpaced the development of new antibiotics, leading to renewed interest in endolysins. Endolysins have been investigated as novel biocontrol agents for Gram-positive bacteria. However, their efficacy against Gram-negative species is limited by the barrier presented by their outer membrane, which prevents endolysin access to the peptidoglycan substrate.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!