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      KCI등재 SCIE SCOPUS

      Characterization of staphylococcal endolysin LysSAP33 possessing untypical domain composition

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      https://www.riss.kr/link?id=A107827076

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      다국어 초록 (Multilingual Abstract)

      Endolysin, a peptidoglycan hydrolase derived from bacteriophage, has been suggested as an alternative antimicrobial agent. Many endolysins on staphylococcal phages have been identified and applied extensively against Staphylococcus spp.
      Among them, LysK-like endolysin, a well-studied staphylococcal endolysin, accounts for most of the identified endolysins.
      However, relatively little interest has been paid to LysKunlike endolysin and a few of them has been characterized.
      An endolysin LysSAP33 encoded on bacteriophage SAP33 shared low homology with LysK-like endolysin in sequence by 41% and domain composition (CHAP-unknown CBD).
      A green fluorescence assay using a fusion protein for Lys- SAP33_CBD indicated that the CBD domain (157-251 aa) was bound to the peptidoglycan of S. aureus. The deletion of LysSAP33_CBD at the C-terminal region resulted in a significant decrease in lytic activity and efficacy. Compared to LysK-like endolysin, LysSAP33 retained its lytic activity in a broader range of temperature, pH, and NaCl concentrations.
      In addition, it showed a higher activity against biofilms than LysK-like endolysin. This study could be a helpful tool to develop our understanding of staphylococcal endolysins not belonging to LysK-like endolysins and a potential biocontrol agent against biofilms.
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      Endolysin, a peptidoglycan hydrolase derived from bacteriophage, has been suggested as an alternative antimicrobial agent. Many endolysins on staphylococcal phages have been identified and applied extensively against Staphylococcus spp. Among them, Ly...

      Endolysin, a peptidoglycan hydrolase derived from bacteriophage, has been suggested as an alternative antimicrobial agent. Many endolysins on staphylococcal phages have been identified and applied extensively against Staphylococcus spp.
      Among them, LysK-like endolysin, a well-studied staphylococcal endolysin, accounts for most of the identified endolysins.
      However, relatively little interest has been paid to LysKunlike endolysin and a few of them has been characterized.
      An endolysin LysSAP33 encoded on bacteriophage SAP33 shared low homology with LysK-like endolysin in sequence by 41% and domain composition (CHAP-unknown CBD).
      A green fluorescence assay using a fusion protein for Lys- SAP33_CBD indicated that the CBD domain (157-251 aa) was bound to the peptidoglycan of S. aureus. The deletion of LysSAP33_CBD at the C-terminal region resulted in a significant decrease in lytic activity and efficacy. Compared to LysK-like endolysin, LysSAP33 retained its lytic activity in a broader range of temperature, pH, and NaCl concentrations.
      In addition, it showed a higher activity against biofilms than LysK-like endolysin. This study could be a helpful tool to develop our understanding of staphylococcal endolysins not belonging to LysK-like endolysins and a potential biocontrol agent against biofilms.

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      참고문헌 (Reference)

      1 Son, B., "The auxiliary role of the amidase domain in cell wall binding and exolytic activity of staphylococcal phage endolysins" 10 : 284-, 2018

      2 Bateman, A., "The CHAP domain : a large family of amidases including GSP amidase and peptidoglycan hydrolases" 28 : 234-237, 2003

      3 Park, Y., "Structure of bacteriophage SPN1S endolysin reveals an unusual two-module fold for the peptidoglycan lytic and binding activity" 92 : 316-325, 2014

      4 Gu, J., "Structural and biochemical characterization reveals LysGH15 as an unprecedented"EF-hand-like"calcium-binding phage lysin" 10 : e1004109-, 2014

      5 Knox, J., "Staphylococcus aureus infections : transmission within households and the community" 23 : 437-444, 2015

      6 Abaev, I., "Staphylococcal phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site" 97 : 3449-3456, 2013

      7 Schmelcher, M., "Rapid multiplex detection and differentiation of Listeria cells by use of fluorescent phage endolysin cell wall binding domains" 76 : 5745-5756, 2010

      8 Horgan, M., "Phage lysin LysK can be truncated to its CHAP domain and retain lytic activity against live antibiotic-resistant staphylococci" 75 : 872-874, 2009

      9 Gupta, R., "P-27/HP endolysin as antibacterial agent for antibiotic resistant Staphylococcus aureus of human infections" 63 : 39-, 2011

      10 Johnson, M., "NCBI BLAST : a better web interface" 36 : W5-, 2008

      1 Son, B., "The auxiliary role of the amidase domain in cell wall binding and exolytic activity of staphylococcal phage endolysins" 10 : 284-, 2018

      2 Bateman, A., "The CHAP domain : a large family of amidases including GSP amidase and peptidoglycan hydrolases" 28 : 234-237, 2003

      3 Park, Y., "Structure of bacteriophage SPN1S endolysin reveals an unusual two-module fold for the peptidoglycan lytic and binding activity" 92 : 316-325, 2014

      4 Gu, J., "Structural and biochemical characterization reveals LysGH15 as an unprecedented"EF-hand-like"calcium-binding phage lysin" 10 : e1004109-, 2014

      5 Knox, J., "Staphylococcus aureus infections : transmission within households and the community" 23 : 437-444, 2015

      6 Abaev, I., "Staphylococcal phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site" 97 : 3449-3456, 2013

      7 Schmelcher, M., "Rapid multiplex detection and differentiation of Listeria cells by use of fluorescent phage endolysin cell wall binding domains" 76 : 5745-5756, 2010

      8 Horgan, M., "Phage lysin LysK can be truncated to its CHAP domain and retain lytic activity against live antibiotic-resistant staphylococci" 75 : 872-874, 2009

      9 Gupta, R., "P-27/HP endolysin as antibacterial agent for antibiotic resistant Staphylococcus aureus of human infections" 63 : 39-, 2011

      10 Johnson, M., "NCBI BLAST : a better web interface" 36 : W5-, 2008

      11 Becker, S. C., "Lytic activity of the staphylolytic Twort phage endolysin CHAP domain is enhanced by the SH3b cell wall binding domain" 362 : 1-8, 2015

      12 Sass, P., "Lytic activity of recombinant bacteriophage φ11 and φ12 endolysins on whole cells and biofilms of Staphylococcus aureus" 73 : 347-352, 2007

      13 Donovan, D. M., "Lysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin" 265 : 133-139, 2006

      14 Kim, S., "LysSAP26, a new recombinant phage endolysin with a broad spectrum antibacterial activity" 12 : 1340-, 2020

      15 Becker, S. C., "LysK CHAP endopeptidase domain is required for lysis of live staphylococcal cells" 294 : 52-60, 2009

      16 Han, J. E., "Isolation and characterization of a Myoviridae bacteriophage against Staphylococcus aureus isolated from dairy cows with mastitis" 95 : 758-763, 2013

      17 Tegel, H., "Increased levels of recombinant human proteins with the Escherichia coli strain Rosetta(DE3)" 69 : 159-167, 2010

      18 Chibli, H., "Immobilized phage proteins for specific detection of staphylococci" 139 : 179-186, 2014

      19 Guo, T., "Functional analysis of the N-terminal region of endolysin Lyb5 encoded by Lactobacillus fermentum bacteriophage φPYB5" 203 : 1-7, 2015

      20 Schmelcher, M., "Evolutionarily distinct bacteriophage endolysins featuring conserved peptidoglycan cleavage sites protect mice from MRSA infection" 70 : 1453-1465, 2015

      21 Gutiérrez, D., "Effective removal of staphylococcal biofilms by the endolysin LysH5" 9 : e107307-, 2014

      22 Sanz-Gaitero, M., "Crystal structure of the lytic CHAPK domain of the endolysin LysK from Staphylococcus aureus bacteriophage K" 11 : 133-, 2014

      23 Selvarasu, S., "Characterizing Escherichia coli DH5αgrowth and metabolism in a complex medium using genomescale flux analysis" 102 : 923-934, 2009

      24 Fujiki, J., "Characterization of the lytic capability of a Lysk-like endolysin, Lys-phiSA012, derived from a polyvalent Staphylococcus aureus bacteriophage" 11 : 25-, 2018

      25 Chang, Y., "Characterization of a novel endolysin LysSA11 and its utility as a potent biocontrol agent against Staphylococcus aureus on food and utensils" 68 : 112-120, 2017

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

      27 Melo, L. D. R., "Characterization of a new Staphylococcus aureus Kayvirus harboring a lysin active against biofilms" 10 : 182-, 2018

      28 유준혁, "Characteristics and Lytic Activity of Phage-Derived Peptidoglycan Hydrolase, LysSAP8, as a Potent Alternative Biocontrol Agent for Staphylococcus aureus" 한국미생물·생명공학회 29 (29): 1916-1924, 2019

      29 Loessner, M. J., "C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates" 44 : 335-349, 2002

      30 Briers, Y., "Breaking barriers : expansion of the use of endolysins as novel antibacterials against Gram-negative bacteria" 10 : 377-390, 2015

      31 Vergara, A., "Biofilm formation and its relationship with the molecular characteristics of food-related Methicillin-Resistant Staphylococcus aureus(MRSA)" 82 : 2364-2370, 2017

      32 Sharma, S., "Bacteriophages and its applications : an overview" 62 : 17-55, 2017

      33 Harper, D. R., "Bacteriophages and biofilms" 3 : 270-284, 2014

      34 Jamal, M., "Bacteriophages : an overview of the control strategies against multiple bacterial infections in different fields" 59 : 123-133, 2019

      35 Fenton, M., "Bacteriophage-derived peptidase CHAPK eliminates and prevents staphylococcal biofilms" 2013 : 625341-, 2013

      36 Wernicki, A., "Bacteriophage therapy to combat bacterial infections in poultry" 14 : 179-, 2017

      37 Schmelcher, M., "Bacteriophage endolysins as novel antimicrobials" 7 : 1147-1171, 2012

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

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      2023 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2020-01-01 평가 등재학술지 유지 (해외등재 학술지 평가) KCI등재
      2013-12-02 학술지명변경 외국어명 : The Journal of Microbiology -> Journal of Microbiology KCI등재
      2010-01-01 평가 등재학술지 유지 (등재유지) KCI등재
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      1999-01-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      2016 1.76 0.2 1.22
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