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      KCI등재 SCIE SCOPUS

      Characterization of thermostable bacteriophage CPD2 and its endolysin LysCPD2 as biocontrol agents against Clostridium perfringens

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      https://www.riss.kr/link?id=A108791079

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      다국어 초록 (Multilingual Abstract)

      Clostridium perfringens is one of the major foodborne pathogens in humans and animals. With the prevalence of antibiotic-resistant C. perfringens strains, bacteriophages and their endolysins have received considerable attention as promising alternatives to antibiotics. In this study, C. perfringens phage CPD2 was isolated from retail chicken samples. CPD2 belongs to the Podoviridae family and exhibits remarkable thermostability. While CPD2 has narrow host specificity, its endolysin LysCPD2 showed a broader lytic range, killing not only C. perfringens strains but other Gram-positive bacteria, such as B. cereus and B. subtilis. In addition, due to its exceptional thermal stability, LysCPD2 showed significant antibacterial ability against germinating C. perfringens spores during the heat activation process (75 °C for 20 min). Taken together, these results indicate that both thermostable phage CPD2 and its endolysin LysCPD2 can be used as efficient antimicrobial agents to control C. perfringens during thermal processing of foods.
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      Clostridium perfringens is one of the major foodborne pathogens in humans and animals. With the prevalence of antibiotic-resistant C. perfringens strains, bacteriophages and their endolysins have received considerable attention as promising alternativ...

      Clostridium perfringens is one of the major foodborne pathogens in humans and animals. With the prevalence of antibiotic-resistant C. perfringens strains, bacteriophages and their endolysins have received considerable attention as promising alternatives to antibiotics. In this study, C. perfringens phage CPD2 was isolated from retail chicken samples. CPD2 belongs to the Podoviridae family and exhibits remarkable thermostability. While CPD2 has narrow host specificity, its endolysin LysCPD2 showed a broader lytic range, killing not only C. perfringens strains but other Gram-positive bacteria, such as B. cereus and B. subtilis. In addition, due to its exceptional thermal stability, LysCPD2 showed significant antibacterial ability against germinating C. perfringens spores during the heat activation process (75 °C for 20 min). Taken together, these results indicate that both thermostable phage CPD2 and its endolysin LysCPD2 can be used as efficient antimicrobial agents to control C. perfringens during thermal processing of foods.

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      참고문헌 (Reference)

      1 Swift SM, "Thermophile lytic enzyme fusion proteins that target Clostridium perfringens" 8 : 214-, 2019

      2 Aziz RK, "The RAST Server : Rapid annotations using subsystems technology" 9 : 1-15, 2008

      3 Strain D, "The Agr-like quorum-sensing system regulates sporulation and production of enterotoxin and beta2 toxin by Clostridium perfringens type A non-food-borne human gastrointestinal disease strain F5603" 79 : 2451-2459, 2011

      4 Henriques AO, "Structure and assembly of the bacterial endospore coat" 20 : 95-110, 2000

      5 Akhtar S, "Strategy to inactivate Clostridium perfringens spores in meat products" 26 : 272-277, 2009

      6 Smith CJ, "Selection and application of natural antimicrobials to control Clostridium perfringens in sous-vide chicken breasts inhibition of C. perfringens in sous-vide chicken" 347 : 109193-, 2021

      7 Fancher CA, "Research Note: Prevalence and molecular characteristics of Clostridium perfringens in “no antibiotics ever” broiler farms" 100 : 101414-, 2021

      8 Kazanavičiūtė V, "Plant-expressed bacteriophage lysins control pathogenic strains of Clostridium perfringens" 8 : 10589-, 2018

      9 Sharma U, "Phage-derived lysins as potential agents for eradicating biofilms and persisters" 23 : 848-856, 2018

      10 Schleifer KH, "Peptidoglycan types of bacterial cell walls and their taxonomic implications" 36 : 407-477, 1972

      1 Swift SM, "Thermophile lytic enzyme fusion proteins that target Clostridium perfringens" 8 : 214-, 2019

      2 Aziz RK, "The RAST Server : Rapid annotations using subsystems technology" 9 : 1-15, 2008

      3 Strain D, "The Agr-like quorum-sensing system regulates sporulation and production of enterotoxin and beta2 toxin by Clostridium perfringens type A non-food-borne human gastrointestinal disease strain F5603" 79 : 2451-2459, 2011

      4 Henriques AO, "Structure and assembly of the bacterial endospore coat" 20 : 95-110, 2000

      5 Akhtar S, "Strategy to inactivate Clostridium perfringens spores in meat products" 26 : 272-277, 2009

      6 Smith CJ, "Selection and application of natural antimicrobials to control Clostridium perfringens in sous-vide chicken breasts inhibition of C. perfringens in sous-vide chicken" 347 : 109193-, 2021

      7 Fancher CA, "Research Note: Prevalence and molecular characteristics of Clostridium perfringens in “no antibiotics ever” broiler farms" 100 : 101414-, 2021

      8 Kazanavičiūtė V, "Plant-expressed bacteriophage lysins control pathogenic strains of Clostridium perfringens" 8 : 10589-, 2018

      9 Sharma U, "Phage-derived lysins as potential agents for eradicating biofilms and persisters" 23 : 848-856, 2018

      10 Schleifer KH, "Peptidoglycan types of bacterial cell walls and their taxonomic implications" 36 : 407-477, 1972

      11 Szweda P, "Peptidoglycan hydrolases-potential weapons against Staphylococcus aureus" 96 : 1157-1174, 2012

      12 Mehdizadeh Gohari I, A, "Pathogenicity and virulence of Clostridium perfringens" 12 : 723-753, 2021

      13 De Jong AEI, "Optimizing sporulation of Clostridium perfringens" 65 : 1457-1462, 2002

      14 Volozhantsev NV, "Molecular characterization of Podoviral bacteriophages virulent for Clostridium perfringens and their comparison with members of the Picovirinae" 7 : 2012

      15 Lewis R, "Isolation of a novel jumbo bacteriophage effective against Klebsiella aerogenes" 7 : 67-, 2020

      16 Fauquet CM, "International Committee on Taxonomy of Viruses and the 3, 142 unassigned species" 2 : 1-10, 2005

      17 Quevillon E, "InterProScan : Protein domains identifier" 33 : 116-120, 2005

      18 Warda AK, "Influence of food matrix on outgrowth heterogeneity of heat damaged Bacillus cereus spores" 201 : 27-34, 2015

      19 Lavigne R, "Identification and characterization of a highly thermostable bacteriophage lysozyme" 61 : 2753-2759, 2004

      20 Andersen KG, "Growth of Heat-Treated Enterotoxin-Positive Clostridium perfringens and the Implications for Safe Cooling Rates" 67 : 83-89, 2004

      21 Zeugin JA, "Ethanol precipitation of DNA" 7 : 1-2, 1985

      22 Lee C, "Development of advanced chimeric endolysin to control multidrug-resistant Staphylococcus aureus through domain shuffling" 7 : 2081-2092, 2021

      23 Thippareddi H, "Control of Clostridium perfringens germination and outgrowth by buffered sodium citrate during chilling of roast beef and injected pork" 66 : 376-381, 2003

      24 Ha E, "Clostridium perfringens virulent bacteriophage CPS2 and its thermostable endolysin lysCPS2" 10 : 1-10, 2018

      25 la Mora ZV De, "Clostridium perfringens as foodborne pathogen in broiler production : Pathophysiology and potential strategies for controlling necrotic enteritis" 10 : 1-28, 2020

      26 Alnoman M, "Chitosan inhibits enterotoxigenic Clostridium perfringens type A in growth medium and chicken meat" 64 : 15-22, 2017

      27 Park H, "Characterization of the lytic phage MSP1 for the inhibition of multidrug-resistant Salmonella enterica serovars Thompson and its biofilm" 110010-, 2022

      28 Walmagh M, "Characterization of five novel endolysins from Gram-negative infecting bacteriophages" 97 : 4369-4375, 2013

      29 Chang Y, "Characterization of a novel cell wall binding domain-containing Staphylococcus aureus endolysin LysSA97" 101 : 147-158, 2017

      30 Fathima B, "Bacteriophage therapy : recent developments and applications of a renaissant weapon" 172 : 103863-, 2021

      31 Fischetti VA, "Bacteriophage lysins as effective antibacterials" 11 : 393-400, 2008

      32 Loessner MJ, "Bacteriophage endolysins-Current state of research and applications" 8 : 480-487, 2005

      33 Schmelcher M, "Bacteriophage endolysins : applications for food safety" 37 : 76-87, 2016

      34 Fischetti VA, "Bacteriophage endolysins : A novel anti-infective to control Gram-positive pathogens" 300 : 357-362, 2010

      35 Lee C, "Bacteriophage and endolysin engineering for biocontrol of food pathogens/pathogens in the food: recent advances and future trends" 1-20, 2022

      36 Wells-Bennik MHJ, "Bacterial spores in food : Survival, emergence, and outgrowth" 7 : 457-482, 2016

      37 Vollmer W, "Bacterial outer membrane evolution via sporulation?" 8 : 14-18, 2012

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