期刊
MICROORGANISMS
卷 10, 期 3, 页码 -出版社
MDPI
DOI: 10.3390/microorganisms10030606
关键词
Salmonella Enteritidis; Salmonella-phage in food; Siphoviridae; siphoviral morphotype; receptor-binding proteins
类别
资金
- ANID FONDECYT [1181167]
- ANID Millennium Science Initiative/Millennium Initiative for Collaborative Research on Bacterial Resistance [NCN17_081]
Salmonellosis is a common zoonotic foodborne disease, and poultry is a major reservoir for the bacteria. This study introduces a newly isolated bacteriophage STGO-35-1, which effectively reduces Salmonella enterica serovar Enteritidis in chicken meat. The phage's genomic and phenotypic characteristics, as well as its potential as a biocontrol agent, are evaluated.
Salmonellosis is one of the most frequently reported zoonotic foodborne diseases worldwide, and poultry is the most important reservoir of Salmonella enterica serovar Enteritidis. The use of lytic bacteriophages (phages) to reduce foodborne pathogens has emerged as a promising biocontrol intervention for Salmonella spp. Here, we describe and evaluate the newly isolated Salmonella phage STGO-35-1, including: (i) genomic and phenotypic characterization, (ii) an analysis of the reduction of Salmonella in chicken meat, and (iii) genome plasticity testing. Phage STGO-35-1 represents an unclassified siphovirus, with a length of 47,483 bp, a G + C content of 46.5%, a headful strategy of packaging, and a virulent lifestyle. Phage STGO-35-1 reduced S. Enteritidis counts in chicken meat by 2.5 orders of magnitude at 4 degrees C. We identified two receptor-binding proteins with affinity to LPS, and their encoding genes showed plasticity during an exposure assay. Phenotypic, proteomic, and genomic characteristics of STGO-35-1, as well as the Salmonella reduction in chicken meat, support the potential use of STGO-35-1 as a targeted biocontrol agent against S. Enteritidis in chicken meat. Additionally, computational analysis and a short exposure time assay allowed us to predict the plasticity of genes encoding putative receptor-binding proteins.
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