Stable expression of bioactive recombinant pleurocidin in a fish cell line
Abstract Pleurocidin (Ple), a linear cationic peptide of 25 amino acids, is a member of a larger family of antimicrobial peptides present in flatfish. Previous studies have shown that Ple displays a strong antimicrobial activity against a broad spectrum of bacteria and appears to play a role in inna...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Brocal, I. [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2006 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2006 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer Berlin Heidelberg, 1984, 72(2006), 6 vom: 25. Apr., Seite 1217-1228 |
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| Übergeordnetes Werk: |
volume:72 ; year:2006 ; number:6 ; day:25 ; month:04 ; pages:1217-1228 |
| Links: |
|---|
| DOI / URN: |
10.1007/s00253-006-0393-7 |
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| Katalog-ID: |
OLC2050708742 |
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| 520 | |a Abstract Pleurocidin (Ple), a linear cationic peptide of 25 amino acids, is a member of a larger family of antimicrobial peptides present in flatfish. Previous studies have shown that Ple displays a strong antimicrobial activity against a broad spectrum of bacteria and appears to play a role in innate host defence. In this work, the genomic sequence encoding the Ple prepropeptide has been isolated from Limandalimanda and cloned in a vector under the control of a non-viral promoter (the carp β-actin promoter). By using this construction, expression of bioactive Ple was demonstrated in transformed fish cell lines continuously growing for more than 2 years. Furthermore, the study of Ple processing, maturation and secretion (by using fusion with green fluorescence protein) and the high bactericidal activity of the secreted recombinant Ple (detectable in cell supernatants without any concentration) are all reported here, as no other recombinant Ple or fish antimicrobial peptide have been expressed before to that extent. Such an overexpression of recombinant Ple or any other related antimicrobial peptide might improve the chances to develop new antibiotic agents, as well as to provide essential information about the mechanism of action, range of activity and the role in the innate immune response of antibiotic peptides. | ||
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| 700 | 1 | |a Perez, L. |4 aut | |
| 700 | 1 | |a Coll, J. M. |4 aut | |
| 700 | 1 | |a Estepa, A. |4 aut | |
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10.1007/s00253-006-0393-7 doi (DE-627)OLC2050708742 (DE-He213)s00253-006-0393-7-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Brocal, I. verfasserin aut Stable expression of bioactive recombinant pleurocidin in a fish cell line 2006 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2006 Abstract Pleurocidin (Ple), a linear cationic peptide of 25 amino acids, is a member of a larger family of antimicrobial peptides present in flatfish. Previous studies have shown that Ple displays a strong antimicrobial activity against a broad spectrum of bacteria and appears to play a role in innate host defence. In this work, the genomic sequence encoding the Ple prepropeptide has been isolated from Limandalimanda and cloned in a vector under the control of a non-viral promoter (the carp β-actin promoter). By using this construction, expression of bioactive Ple was demonstrated in transformed fish cell lines continuously growing for more than 2 years. Furthermore, the study of Ple processing, maturation and secretion (by using fusion with green fluorescence protein) and the high bactericidal activity of the secreted recombinant Ple (detectable in cell supernatants without any concentration) are all reported here, as no other recombinant Ple or fish antimicrobial peptide have been expressed before to that extent. Such an overexpression of recombinant Ple or any other related antimicrobial peptide might improve the chances to develop new antibiotic agents, as well as to provide essential information about the mechanism of action, range of activity and the role in the innate immune response of antibiotic peptides. Green Fluorescence Protein Cell Culture Supernatant Green Fluorescence Protein Expression Transgenic Fish Fish Cell Line Falco, A. aut Mas, V. aut Rocha, A. aut Perez, L. aut Coll, J. M. aut Estepa, A. aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 72(2006), 6 vom: 25. Apr., Seite 1217-1228 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:72 year:2006 number:6 day:25 month:04 pages:1217-1228 https://doi.org/10.1007/s00253-006-0393-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 72 2006 6 25 04 1217-1228 |
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10.1007/s00253-006-0393-7 doi (DE-627)OLC2050708742 (DE-He213)s00253-006-0393-7-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Brocal, I. verfasserin aut Stable expression of bioactive recombinant pleurocidin in a fish cell line 2006 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2006 Abstract Pleurocidin (Ple), a linear cationic peptide of 25 amino acids, is a member of a larger family of antimicrobial peptides present in flatfish. Previous studies have shown that Ple displays a strong antimicrobial activity against a broad spectrum of bacteria and appears to play a role in innate host defence. In this work, the genomic sequence encoding the Ple prepropeptide has been isolated from Limandalimanda and cloned in a vector under the control of a non-viral promoter (the carp β-actin promoter). By using this construction, expression of bioactive Ple was demonstrated in transformed fish cell lines continuously growing for more than 2 years. Furthermore, the study of Ple processing, maturation and secretion (by using fusion with green fluorescence protein) and the high bactericidal activity of the secreted recombinant Ple (detectable in cell supernatants without any concentration) are all reported here, as no other recombinant Ple or fish antimicrobial peptide have been expressed before to that extent. Such an overexpression of recombinant Ple or any other related antimicrobial peptide might improve the chances to develop new antibiotic agents, as well as to provide essential information about the mechanism of action, range of activity and the role in the innate immune response of antibiotic peptides. Green Fluorescence Protein Cell Culture Supernatant Green Fluorescence Protein Expression Transgenic Fish Fish Cell Line Falco, A. aut Mas, V. aut Rocha, A. aut Perez, L. aut Coll, J. M. aut Estepa, A. aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 72(2006), 6 vom: 25. Apr., Seite 1217-1228 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:72 year:2006 number:6 day:25 month:04 pages:1217-1228 https://doi.org/10.1007/s00253-006-0393-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 72 2006 6 25 04 1217-1228 |
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10.1007/s00253-006-0393-7 doi (DE-627)OLC2050708742 (DE-He213)s00253-006-0393-7-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Brocal, I. verfasserin aut Stable expression of bioactive recombinant pleurocidin in a fish cell line 2006 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2006 Abstract Pleurocidin (Ple), a linear cationic peptide of 25 amino acids, is a member of a larger family of antimicrobial peptides present in flatfish. Previous studies have shown that Ple displays a strong antimicrobial activity against a broad spectrum of bacteria and appears to play a role in innate host defence. In this work, the genomic sequence encoding the Ple prepropeptide has been isolated from Limandalimanda and cloned in a vector under the control of a non-viral promoter (the carp β-actin promoter). By using this construction, expression of bioactive Ple was demonstrated in transformed fish cell lines continuously growing for more than 2 years. Furthermore, the study of Ple processing, maturation and secretion (by using fusion with green fluorescence protein) and the high bactericidal activity of the secreted recombinant Ple (detectable in cell supernatants without any concentration) are all reported here, as no other recombinant Ple or fish antimicrobial peptide have been expressed before to that extent. Such an overexpression of recombinant Ple or any other related antimicrobial peptide might improve the chances to develop new antibiotic agents, as well as to provide essential information about the mechanism of action, range of activity and the role in the innate immune response of antibiotic peptides. Green Fluorescence Protein Cell Culture Supernatant Green Fluorescence Protein Expression Transgenic Fish Fish Cell Line Falco, A. aut Mas, V. aut Rocha, A. aut Perez, L. aut Coll, J. M. aut Estepa, A. aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 72(2006), 6 vom: 25. Apr., Seite 1217-1228 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:72 year:2006 number:6 day:25 month:04 pages:1217-1228 https://doi.org/10.1007/s00253-006-0393-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 72 2006 6 25 04 1217-1228 |
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10.1007/s00253-006-0393-7 doi (DE-627)OLC2050708742 (DE-He213)s00253-006-0393-7-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Brocal, I. verfasserin aut Stable expression of bioactive recombinant pleurocidin in a fish cell line 2006 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2006 Abstract Pleurocidin (Ple), a linear cationic peptide of 25 amino acids, is a member of a larger family of antimicrobial peptides present in flatfish. Previous studies have shown that Ple displays a strong antimicrobial activity against a broad spectrum of bacteria and appears to play a role in innate host defence. In this work, the genomic sequence encoding the Ple prepropeptide has been isolated from Limandalimanda and cloned in a vector under the control of a non-viral promoter (the carp β-actin promoter). By using this construction, expression of bioactive Ple was demonstrated in transformed fish cell lines continuously growing for more than 2 years. Furthermore, the study of Ple processing, maturation and secretion (by using fusion with green fluorescence protein) and the high bactericidal activity of the secreted recombinant Ple (detectable in cell supernatants without any concentration) are all reported here, as no other recombinant Ple or fish antimicrobial peptide have been expressed before to that extent. Such an overexpression of recombinant Ple or any other related antimicrobial peptide might improve the chances to develop new antibiotic agents, as well as to provide essential information about the mechanism of action, range of activity and the role in the innate immune response of antibiotic peptides. Green Fluorescence Protein Cell Culture Supernatant Green Fluorescence Protein Expression Transgenic Fish Fish Cell Line Falco, A. aut Mas, V. aut Rocha, A. aut Perez, L. aut Coll, J. M. aut Estepa, A. aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 72(2006), 6 vom: 25. Apr., Seite 1217-1228 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:72 year:2006 number:6 day:25 month:04 pages:1217-1228 https://doi.org/10.1007/s00253-006-0393-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 72 2006 6 25 04 1217-1228 |
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10.1007/s00253-006-0393-7 doi (DE-627)OLC2050708742 (DE-He213)s00253-006-0393-7-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Brocal, I. verfasserin aut Stable expression of bioactive recombinant pleurocidin in a fish cell line 2006 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2006 Abstract Pleurocidin (Ple), a linear cationic peptide of 25 amino acids, is a member of a larger family of antimicrobial peptides present in flatfish. Previous studies have shown that Ple displays a strong antimicrobial activity against a broad spectrum of bacteria and appears to play a role in innate host defence. In this work, the genomic sequence encoding the Ple prepropeptide has been isolated from Limandalimanda and cloned in a vector under the control of a non-viral promoter (the carp β-actin promoter). By using this construction, expression of bioactive Ple was demonstrated in transformed fish cell lines continuously growing for more than 2 years. Furthermore, the study of Ple processing, maturation and secretion (by using fusion with green fluorescence protein) and the high bactericidal activity of the secreted recombinant Ple (detectable in cell supernatants without any concentration) are all reported here, as no other recombinant Ple or fish antimicrobial peptide have been expressed before to that extent. Such an overexpression of recombinant Ple or any other related antimicrobial peptide might improve the chances to develop new antibiotic agents, as well as to provide essential information about the mechanism of action, range of activity and the role in the innate immune response of antibiotic peptides. Green Fluorescence Protein Cell Culture Supernatant Green Fluorescence Protein Expression Transgenic Fish Fish Cell Line Falco, A. aut Mas, V. aut Rocha, A. aut Perez, L. aut Coll, J. M. aut Estepa, A. aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 72(2006), 6 vom: 25. Apr., Seite 1217-1228 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:72 year:2006 number:6 day:25 month:04 pages:1217-1228 https://doi.org/10.1007/s00253-006-0393-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 72 2006 6 25 04 1217-1228 |
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Enthalten in Applied microbiology and biotechnology 72(2006), 6 vom: 25. Apr., Seite 1217-1228 volume:72 year:2006 number:6 day:25 month:04 pages:1217-1228 |
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stable expression of bioactive recombinant pleurocidin in a fish cell line |
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Stable expression of bioactive recombinant pleurocidin in a fish cell line |
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Abstract Pleurocidin (Ple), a linear cationic peptide of 25 amino acids, is a member of a larger family of antimicrobial peptides present in flatfish. Previous studies have shown that Ple displays a strong antimicrobial activity against a broad spectrum of bacteria and appears to play a role in innate host defence. In this work, the genomic sequence encoding the Ple prepropeptide has been isolated from Limandalimanda and cloned in a vector under the control of a non-viral promoter (the carp β-actin promoter). By using this construction, expression of bioactive Ple was demonstrated in transformed fish cell lines continuously growing for more than 2 years. Furthermore, the study of Ple processing, maturation and secretion (by using fusion with green fluorescence protein) and the high bactericidal activity of the secreted recombinant Ple (detectable in cell supernatants without any concentration) are all reported here, as no other recombinant Ple or fish antimicrobial peptide have been expressed before to that extent. Such an overexpression of recombinant Ple or any other related antimicrobial peptide might improve the chances to develop new antibiotic agents, as well as to provide essential information about the mechanism of action, range of activity and the role in the innate immune response of antibiotic peptides. © Springer-Verlag 2006 |
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Abstract Pleurocidin (Ple), a linear cationic peptide of 25 amino acids, is a member of a larger family of antimicrobial peptides present in flatfish. Previous studies have shown that Ple displays a strong antimicrobial activity against a broad spectrum of bacteria and appears to play a role in innate host defence. In this work, the genomic sequence encoding the Ple prepropeptide has been isolated from Limandalimanda and cloned in a vector under the control of a non-viral promoter (the carp β-actin promoter). By using this construction, expression of bioactive Ple was demonstrated in transformed fish cell lines continuously growing for more than 2 years. Furthermore, the study of Ple processing, maturation and secretion (by using fusion with green fluorescence protein) and the high bactericidal activity of the secreted recombinant Ple (detectable in cell supernatants without any concentration) are all reported here, as no other recombinant Ple or fish antimicrobial peptide have been expressed before to that extent. Such an overexpression of recombinant Ple or any other related antimicrobial peptide might improve the chances to develop new antibiotic agents, as well as to provide essential information about the mechanism of action, range of activity and the role in the innate immune response of antibiotic peptides. © Springer-Verlag 2006 |
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Abstract Pleurocidin (Ple), a linear cationic peptide of 25 amino acids, is a member of a larger family of antimicrobial peptides present in flatfish. Previous studies have shown that Ple displays a strong antimicrobial activity against a broad spectrum of bacteria and appears to play a role in innate host defence. In this work, the genomic sequence encoding the Ple prepropeptide has been isolated from Limandalimanda and cloned in a vector under the control of a non-viral promoter (the carp β-actin promoter). By using this construction, expression of bioactive Ple was demonstrated in transformed fish cell lines continuously growing for more than 2 years. Furthermore, the study of Ple processing, maturation and secretion (by using fusion with green fluorescence protein) and the high bactericidal activity of the secreted recombinant Ple (detectable in cell supernatants without any concentration) are all reported here, as no other recombinant Ple or fish antimicrobial peptide have been expressed before to that extent. Such an overexpression of recombinant Ple or any other related antimicrobial peptide might improve the chances to develop new antibiotic agents, as well as to provide essential information about the mechanism of action, range of activity and the role in the innate immune response of antibiotic peptides. © Springer-Verlag 2006 |
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