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The effectiveness of endolysin ENDO-1252 from Salmonella bacteriophage-1252 against nontyphoidal Salmonella enterica.
Tung, Chuan-Wei; Julianingsih, Dita; Canagarajah, Christa; Sellers, George; Scriba, Aaron; Alvarado-Martínez, Zabdiel; Tabashsum, Zajeba; Biswas, Debabrata.
Affiliation
  • Tung CW; Department of Animal and Avian Sciences, University of Maryland, College Park, MD 20740, United States.
  • Julianingsih D; Department of Animal and Avian Sciences, University of Maryland, College Park, MD 20740, United States.
  • Canagarajah C; Department of Biology, University of Maryland, College Park, College Park, MD 20740, United States.
  • Sellers G; Department of Biology, University of Maryland, College Park, College Park, MD 20740, United States.
  • Scriba A; Department of Biology, University of Maryland, College Park, College Park, MD 20740, United States.
  • Alvarado-Martínez Z; Biological Sciences Program-Molecular and Cellular Biology, University of Maryland, College Park, MD 20740, United States.
  • Tabashsum Z; Biological Sciences Program-Molecular and Cellular Biology, University of Maryland, College Park, MD 20740, United States.
  • Biswas D; Department of Animal and Avian Sciences, University of Maryland, College Park, MD 20740, United States.
FEMS Microbiol Lett ; 3712024 Jan 09.
Article in En | MEDLINE | ID: mdl-38970360
ABSTRACT
Salmonella enterica (S. enterica) is the most common food and waterborne pathogen worldwide. The growing trend of antibiotic-resistant S. enterica poses severe healthcare threats. As an alternative antimicrobial agent, bacteriophage-encoded endolysins (endolysins) are a potential agent in controlling S. enterica infection. Endolysins are enzymes that particularly target the peptidoglycan layer of bacterial cells, leading to their rupture and destruction. However, the application of endolysins against Gram-negative bacteria is limited due to the presence of the outer membrane in the cell wall, which hinders the permeation of externally applied endolysins. This study aimed the prokaryotic expression system to produce the recombinant endolysin ENDO-1252, encoded by the Salmonella bacteriophage-1252 associated with S. Enteritidis. Subsequently, ENDO-1252 had strong lytic activity not only against S. Enteritidis but also against S. Typhimurium. In addition, ENDO-1252 showed optimal thermostability and lytic activity at 25°C with a pH of 7.0. In combination with 0.1 mM EDTA, the effect of 120 µg of ENDO-1252 for 6 hours exhibited the highest lytic activity, resulting in a reduction of 1.15 log or 92.87% on S. Enteritidis. These findings suggest that ENDO-1252 can be used as a potential and innovative antibacterial agent for controlling the growth of S. Enteritidis.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Endopeptidases / Salmonella Phages / Salmonella enterica Language: En Journal: FEMS Microbiol Lett Year: 2024 Document type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Endopeptidases / Salmonella Phages / Salmonella enterica Language: En Journal: FEMS Microbiol Lett Year: 2024 Document type: Article Affiliation country: United States