Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk

Abstract A novel endogenous peptide cleaved from 197–213 AA of β-casein, named β-casein 197, was identified by tandem mass spectrometry. β-casein 197 constituted a significant proportion of the peptide content in preterm milk. This study investigated the antibacterial effects and mechanisms against...
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Gespeichert in:

Autor*in:	Fu, Yanrong [verfasserIn] Ji, Chenbo [verfasserIn] Chen, Xiaohui [verfasserIn] Cui, Xianwei [verfasserIn] Wang, Xing [verfasserIn] Feng, Jie [verfasserIn] Li, Yun [verfasserIn] Qin, Rui [verfasserIn] Guo, Xirong [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	Human milk β-Casein 197 Common pathogenic bacteria Antibacterial effect

Übergeordnetes Werk:	Enthalten in: AMB express - Heidelberg : Springer, 2011, 7(2017), 1 vom: 06. Juni
Übergeordnetes Werk:	volume:7 ; year:2017 ; number:1 ; day:06 ; month:06

Links:	Volltext

DOI / URN:	10.1186/s13568-017-0409-y

Katalog-ID:	SPR031832075

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520			\|a Abstract A novel endogenous peptide cleaved from 197–213 AA of β-casein, named β-casein 197, was identified by tandem mass spectrometry. β-casein 197 constituted a significant proportion of the peptide content in preterm milk. This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. Scanning electron and transmission electron microscopy revealed affected extracellular and intracellular structure for three species of bacteria, while a DNA-binding assay showed that the antimicrobial activity did not occur through DNA binding. This study suggests that β-casein 197 has antimicrobial activity against common pathogenic bacteria in newborns with infection. The peptide induced membrane permeabilization but did not bind to genomic DNA. Based on our findings, β-casein 197 has potential clinical value for preventing infections of premature infants.
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allfields	10.1186/s13568-017-0409-y doi (DE-627)SPR031832075 (SPR)s13568-017-0409-y-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Fu, Yanrong verfasserin aut Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A novel endogenous peptide cleaved from 197–213 AA of β-casein, named β-casein 197, was identified by tandem mass spectrometry. β-casein 197 constituted a significant proportion of the peptide content in preterm milk. This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. Scanning electron and transmission electron microscopy revealed affected extracellular and intracellular structure for three species of bacteria, while a DNA-binding assay showed that the antimicrobial activity did not occur through DNA binding. This study suggests that β-casein 197 has antimicrobial activity against common pathogenic bacteria in newborns with infection. The peptide induced membrane permeabilization but did not bind to genomic DNA. Based on our findings, β-casein 197 has potential clinical value for preventing infections of premature infants. Human milk (dpeaa)DE-He213 β-Casein 197 (dpeaa)DE-He213 Common pathogenic bacteria (dpeaa)DE-He213 Antibacterial effect (dpeaa)DE-He213 Ji, Chenbo verfasserin aut Chen, Xiaohui verfasserin aut Cui, Xianwei verfasserin aut Wang, Xing verfasserin aut Feng, Jie verfasserin aut Li, Yun verfasserin aut Qin, Rui verfasserin aut Guo, Xirong verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 7(2017), 1 vom: 06. Juni (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:7 year:2017 number:1 day:06 month:06 https://dx.doi.org/10.1186/s13568-017-0409-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 58.30 ASE AR 7 2017 1 06 06
spelling	10.1186/s13568-017-0409-y doi (DE-627)SPR031832075 (SPR)s13568-017-0409-y-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Fu, Yanrong verfasserin aut Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A novel endogenous peptide cleaved from 197–213 AA of β-casein, named β-casein 197, was identified by tandem mass spectrometry. β-casein 197 constituted a significant proportion of the peptide content in preterm milk. This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. Scanning electron and transmission electron microscopy revealed affected extracellular and intracellular structure for three species of bacteria, while a DNA-binding assay showed that the antimicrobial activity did not occur through DNA binding. This study suggests that β-casein 197 has antimicrobial activity against common pathogenic bacteria in newborns with infection. The peptide induced membrane permeabilization but did not bind to genomic DNA. Based on our findings, β-casein 197 has potential clinical value for preventing infections of premature infants. Human milk (dpeaa)DE-He213 β-Casein 197 (dpeaa)DE-He213 Common pathogenic bacteria (dpeaa)DE-He213 Antibacterial effect (dpeaa)DE-He213 Ji, Chenbo verfasserin aut Chen, Xiaohui verfasserin aut Cui, Xianwei verfasserin aut Wang, Xing verfasserin aut Feng, Jie verfasserin aut Li, Yun verfasserin aut Qin, Rui verfasserin aut Guo, Xirong verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 7(2017), 1 vom: 06. Juni (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:7 year:2017 number:1 day:06 month:06 https://dx.doi.org/10.1186/s13568-017-0409-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 58.30 ASE AR 7 2017 1 06 06
allfields_unstemmed	10.1186/s13568-017-0409-y doi (DE-627)SPR031832075 (SPR)s13568-017-0409-y-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Fu, Yanrong verfasserin aut Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A novel endogenous peptide cleaved from 197–213 AA of β-casein, named β-casein 197, was identified by tandem mass spectrometry. β-casein 197 constituted a significant proportion of the peptide content in preterm milk. This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. Scanning electron and transmission electron microscopy revealed affected extracellular and intracellular structure for three species of bacteria, while a DNA-binding assay showed that the antimicrobial activity did not occur through DNA binding. This study suggests that β-casein 197 has antimicrobial activity against common pathogenic bacteria in newborns with infection. The peptide induced membrane permeabilization but did not bind to genomic DNA. Based on our findings, β-casein 197 has potential clinical value for preventing infections of premature infants. Human milk (dpeaa)DE-He213 β-Casein 197 (dpeaa)DE-He213 Common pathogenic bacteria (dpeaa)DE-He213 Antibacterial effect (dpeaa)DE-He213 Ji, Chenbo verfasserin aut Chen, Xiaohui verfasserin aut Cui, Xianwei verfasserin aut Wang, Xing verfasserin aut Feng, Jie verfasserin aut Li, Yun verfasserin aut Qin, Rui verfasserin aut Guo, Xirong verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 7(2017), 1 vom: 06. Juni (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:7 year:2017 number:1 day:06 month:06 https://dx.doi.org/10.1186/s13568-017-0409-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 58.30 ASE AR 7 2017 1 06 06
allfieldsGer	10.1186/s13568-017-0409-y doi (DE-627)SPR031832075 (SPR)s13568-017-0409-y-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Fu, Yanrong verfasserin aut Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A novel endogenous peptide cleaved from 197–213 AA of β-casein, named β-casein 197, was identified by tandem mass spectrometry. β-casein 197 constituted a significant proportion of the peptide content in preterm milk. This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. Scanning electron and transmission electron microscopy revealed affected extracellular and intracellular structure for three species of bacteria, while a DNA-binding assay showed that the antimicrobial activity did not occur through DNA binding. This study suggests that β-casein 197 has antimicrobial activity against common pathogenic bacteria in newborns with infection. The peptide induced membrane permeabilization but did not bind to genomic DNA. Based on our findings, β-casein 197 has potential clinical value for preventing infections of premature infants. Human milk (dpeaa)DE-He213 β-Casein 197 (dpeaa)DE-He213 Common pathogenic bacteria (dpeaa)DE-He213 Antibacterial effect (dpeaa)DE-He213 Ji, Chenbo verfasserin aut Chen, Xiaohui verfasserin aut Cui, Xianwei verfasserin aut Wang, Xing verfasserin aut Feng, Jie verfasserin aut Li, Yun verfasserin aut Qin, Rui verfasserin aut Guo, Xirong verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 7(2017), 1 vom: 06. Juni (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:7 year:2017 number:1 day:06 month:06 https://dx.doi.org/10.1186/s13568-017-0409-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 58.30 ASE AR 7 2017 1 06 06
allfieldsSound	10.1186/s13568-017-0409-y doi (DE-627)SPR031832075 (SPR)s13568-017-0409-y-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl Fu, Yanrong verfasserin aut Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A novel endogenous peptide cleaved from 197–213 AA of β-casein, named β-casein 197, was identified by tandem mass spectrometry. β-casein 197 constituted a significant proportion of the peptide content in preterm milk. This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. Scanning electron and transmission electron microscopy revealed affected extracellular and intracellular structure for three species of bacteria, while a DNA-binding assay showed that the antimicrobial activity did not occur through DNA binding. This study suggests that β-casein 197 has antimicrobial activity against common pathogenic bacteria in newborns with infection. The peptide induced membrane permeabilization but did not bind to genomic DNA. Based on our findings, β-casein 197 has potential clinical value for preventing infections of premature infants. Human milk (dpeaa)DE-He213 β-Casein 197 (dpeaa)DE-He213 Common pathogenic bacteria (dpeaa)DE-He213 Antibacterial effect (dpeaa)DE-He213 Ji, Chenbo verfasserin aut Chen, Xiaohui verfasserin aut Cui, Xianwei verfasserin aut Wang, Xing verfasserin aut Feng, Jie verfasserin aut Li, Yun verfasserin aut Qin, Rui verfasserin aut Guo, Xirong verfasserin aut Enthalten in AMB express Heidelberg : Springer, 2011 7(2017), 1 vom: 06. Juni (DE-627)665672926 (DE-600)2621432-5 2191-0855 nnns volume:7 year:2017 number:1 day:06 month:06 https://dx.doi.org/10.1186/s13568-017-0409-y kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 58.30 ASE AR 7 2017 1 06 06
language	English
source	Enthalten in AMB express 7(2017), 1 vom: 06. Juni volume:7 year:2017 number:1 day:06 month:06
sourceStr	Enthalten in AMB express 7(2017), 1 vom: 06. Juni volume:7 year:2017 number:1 day:06 month:06
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Human milk β-Casein 197 Common pathogenic bacteria Antibacterial effect
dewey-raw	570
isfreeaccess_bool	true
container_title	AMB express
authorswithroles_txt_mv	Fu, Yanrong @@aut@@ Ji, Chenbo @@aut@@ Chen, Xiaohui @@aut@@ Cui, Xianwei @@aut@@ Wang, Xing @@aut@@ Feng, Jie @@aut@@ Li, Yun @@aut@@ Qin, Rui @@aut@@ Guo, Xirong @@aut@@
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This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. 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author	Fu, Yanrong
spellingShingle	Fu, Yanrong ddc 570 bkl 58.30 misc Human milk misc β-Casein 197 misc Common pathogenic bacteria misc Antibacterial effect Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk
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topic_title	570 ASE 58.30 bkl Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk Human milk (dpeaa)DE-He213 β-Casein 197 (dpeaa)DE-He213 Common pathogenic bacteria (dpeaa)DE-He213 Antibacterial effect (dpeaa)DE-He213
topic	ddc 570 bkl 58.30 misc Human milk misc β-Casein 197 misc Common pathogenic bacteria misc Antibacterial effect
topic_unstemmed	ddc 570 bkl 58.30 misc Human milk misc β-Casein 197 misc Common pathogenic bacteria misc Antibacterial effect
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title	Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk
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title_full	Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk
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author_browse	Fu, Yanrong Ji, Chenbo Chen, Xiaohui Cui, Xianwei Wang, Xing Feng, Jie Li, Yun Qin, Rui Guo, Xirong
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class	570 ASE 58.30 bkl
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title_sort	investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk
title_auth	Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk
abstract	Abstract A novel endogenous peptide cleaved from 197–213 AA of β-casein, named β-casein 197, was identified by tandem mass spectrometry. β-casein 197 constituted a significant proportion of the peptide content in preterm milk. This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. Scanning electron and transmission electron microscopy revealed affected extracellular and intracellular structure for three species of bacteria, while a DNA-binding assay showed that the antimicrobial activity did not occur through DNA binding. This study suggests that β-casein 197 has antimicrobial activity against common pathogenic bacteria in newborns with infection. The peptide induced membrane permeabilization but did not bind to genomic DNA. Based on our findings, β-casein 197 has potential clinical value for preventing infections of premature infants.
abstractGer	Abstract A novel endogenous peptide cleaved from 197–213 AA of β-casein, named β-casein 197, was identified by tandem mass spectrometry. β-casein 197 constituted a significant proportion of the peptide content in preterm milk. This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. Scanning electron and transmission electron microscopy revealed affected extracellular and intracellular structure for three species of bacteria, while a DNA-binding assay showed that the antimicrobial activity did not occur through DNA binding. This study suggests that β-casein 197 has antimicrobial activity against common pathogenic bacteria in newborns with infection. The peptide induced membrane permeabilization but did not bind to genomic DNA. Based on our findings, β-casein 197 has potential clinical value for preventing infections of premature infants.
abstract_unstemmed	Abstract A novel endogenous peptide cleaved from 197–213 AA of β-casein, named β-casein 197, was identified by tandem mass spectrometry. β-casein 197 constituted a significant proportion of the peptide content in preterm milk. This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. Scanning electron and transmission electron microscopy revealed affected extracellular and intracellular structure for three species of bacteria, while a DNA-binding assay showed that the antimicrobial activity did not occur through DNA binding. This study suggests that β-casein 197 has antimicrobial activity against common pathogenic bacteria in newborns with infection. The peptide induced membrane permeabilization but did not bind to genomic DNA. Based on our findings, β-casein 197 has potential clinical value for preventing infections of premature infants.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
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title_short	Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk
url	https://dx.doi.org/10.1186/s13568-017-0409-y
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author2	Ji, Chenbo Chen, Xiaohui Cui, Xianwei Wang, Xing Feng, Jie Li, Yun Qin, Rui Guo, Xirong
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up_date	2024-07-04T01:26:16.513Z
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This study investigated the antibacterial effects and mechanisms against common pathogenic bacteria. Six bacterial strains were selected for this study: Escherichia coli, Staphylococcus aureus, Yersinia enterocolitica, Listeria monocytogenes, Klebsiella pneumonia and Bacillus subtilis. After synthesis, serial twofold dilutions of β-casein 197 were added to select for sensitive bacteria. The disk diffusion method and analysis of bacterial staining were used to identify antibacterial effect, while DNA-binding, scanning electron microscopy and transmission electron microscopy were used to explore antimicrobial mechanisms. Disk diffusion showed that E. coli, S. aureus and Y. enterocolitica were sensitive to the β-casein 197. In addition, live/dead fluorescent staining also confirmed antibacterial effects. Scanning electron and transmission electron microscopy revealed affected extracellular and intracellular structure for three species of bacteria, while a DNA-binding assay showed that the antimicrobial activity did not occur through DNA binding. This study suggests that β-casein 197 has antimicrobial activity against common pathogenic bacteria in newborns with infection. The peptide induced membrane permeabilization but did not bind to genomic DNA. 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Investigation into the antimicrobial action and mechanism of a novel endogenous peptide β-casein 197 from human milk

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