Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp.
Abstract Previously we reported an antifungal protein specific to Pythium porphyrae, a causative agent of red rot disease afflicting seaweed Porphyra spp. This study was carried out to identify the antifungal mechanism of the antifungal protein to P. porphyrae. When we first examined the effect of a...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Woo, J.-H. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2003 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2003 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Berlin : Springer, 1975, 62(2003), 4 vom: 23. Mai, Seite 407-413 |
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| Übergeordnetes Werk: |
volume:62 ; year:2003 ; number:4 ; day:23 ; month:05 ; pages:407-413 |
| Links: |
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| DOI / URN: |
10.1007/s00253-003-1235-5 |
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| Katalog-ID: |
SPR002931869 |
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| 041 | |a eng | ||
| 100 | 1 | |a Woo, J.-H. |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp. |
| 264 | 1 | |c 2003 | |
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| 500 | |a © Springer-Verlag 2003 | ||
| 520 | |a Abstract Previously we reported an antifungal protein specific to Pythium porphyrae, a causative agent of red rot disease afflicting seaweed Porphyra spp. This study was carried out to identify the antifungal mechanism of the antifungal protein to P. porphyrae. When we first examined the effect of an anti-Pythium protein (SAP) on the P. porphyrae cell walls, SAP did not decompose the six structural polysaccharides in Pythium cell walls. However, hyphal growth was significantly inhibited in Pythium cells treated with 50 μg/ml of SAP by MTT assay. Protoplasmic leakage was observed in P. porphyrae hyphae treated with SAP for 1 h, followed by hyphal swelling and disintegration, using SYTOX Green, and SAP permeabilized the membrane of P. porphyrae in a dose-dependent manner. Treating P. porphyrae cells with SAP in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP), a membrane-depolarizing agent, significantly reduced the membrane permeability to SYTOX Green. Moreover, a similar effect was observed when the P. porphyrae cells were treated with SAP in the presence of $ MgCl_{2} $. In contrast, identical treatment in the presence of KCl significantly increased the membrane permeability to SYTOX Green. These results suggested that anti-Pythium mechanism of SAP was related to alteration of the membrane permeability in P. porphyrae. | ||
| 650 | 4 | |a Glucan |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Antifungal Protein |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Alcaligenes Faecalis |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Strain AP77 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Antifungal Mechanism |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Kamei, Y. |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Applied microbiology and biotechnology |d Berlin : Springer, 1975 |g 62(2003), 4 vom: 23. Mai, Seite 407-413 |w (DE-627)265509564 |w (DE-600)1464336-4 |x 1432-0614 |7 nnns |
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| 912 | |a GBV_ILN_2027 | ||
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| 912 | |a GBV_ILN_2037 | ||
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| 912 | |a GBV_ILN_2044 | ||
| 912 | |a GBV_ILN_2048 | ||
| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2055 | ||
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| 912 | |a GBV_ILN_2110 | ||
| 912 | |a GBV_ILN_2113 | ||
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| 912 | |a GBV_ILN_2119 | ||
| 912 | |a GBV_ILN_2129 | ||
| 912 | |a GBV_ILN_2143 | ||
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| 912 | |a GBV_ILN_2147 | ||
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10.1007/s00253-003-1235-5 doi (DE-627)SPR002931869 (SPR)s00253-003-1235-5-e DE-627 ger DE-627 rakwb eng Woo, J.-H. verfasserin aut Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp. 2003 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2003 Abstract Previously we reported an antifungal protein specific to Pythium porphyrae, a causative agent of red rot disease afflicting seaweed Porphyra spp. This study was carried out to identify the antifungal mechanism of the antifungal protein to P. porphyrae. When we first examined the effect of an anti-Pythium protein (SAP) on the P. porphyrae cell walls, SAP did not decompose the six structural polysaccharides in Pythium cell walls. However, hyphal growth was significantly inhibited in Pythium cells treated with 50 μg/ml of SAP by MTT assay. Protoplasmic leakage was observed in P. porphyrae hyphae treated with SAP for 1 h, followed by hyphal swelling and disintegration, using SYTOX Green, and SAP permeabilized the membrane of P. porphyrae in a dose-dependent manner. Treating P. porphyrae cells with SAP in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP), a membrane-depolarizing agent, significantly reduced the membrane permeability to SYTOX Green. Moreover, a similar effect was observed when the P. porphyrae cells were treated with SAP in the presence of $ MgCl_{2} $. In contrast, identical treatment in the presence of KCl significantly increased the membrane permeability to SYTOX Green. These results suggested that anti-Pythium mechanism of SAP was related to alteration of the membrane permeability in P. porphyrae. Glucan (dpeaa)DE-He213 Antifungal Protein (dpeaa)DE-He213 Alcaligenes Faecalis (dpeaa)DE-He213 Strain AP77 (dpeaa)DE-He213 Antifungal Mechanism (dpeaa)DE-He213 Kamei, Y. aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 62(2003), 4 vom: 23. Mai, Seite 407-413 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:62 year:2003 number:4 day:23 month:05 pages:407-413 https://dx.doi.org/10.1007/s00253-003-1235-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 62 2003 4 23 05 407-413 |
| spelling |
10.1007/s00253-003-1235-5 doi (DE-627)SPR002931869 (SPR)s00253-003-1235-5-e DE-627 ger DE-627 rakwb eng Woo, J.-H. verfasserin aut Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp. 2003 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2003 Abstract Previously we reported an antifungal protein specific to Pythium porphyrae, a causative agent of red rot disease afflicting seaweed Porphyra spp. This study was carried out to identify the antifungal mechanism of the antifungal protein to P. porphyrae. When we first examined the effect of an anti-Pythium protein (SAP) on the P. porphyrae cell walls, SAP did not decompose the six structural polysaccharides in Pythium cell walls. However, hyphal growth was significantly inhibited in Pythium cells treated with 50 μg/ml of SAP by MTT assay. Protoplasmic leakage was observed in P. porphyrae hyphae treated with SAP for 1 h, followed by hyphal swelling and disintegration, using SYTOX Green, and SAP permeabilized the membrane of P. porphyrae in a dose-dependent manner. Treating P. porphyrae cells with SAP in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP), a membrane-depolarizing agent, significantly reduced the membrane permeability to SYTOX Green. Moreover, a similar effect was observed when the P. porphyrae cells were treated with SAP in the presence of $ MgCl_{2} $. In contrast, identical treatment in the presence of KCl significantly increased the membrane permeability to SYTOX Green. These results suggested that anti-Pythium mechanism of SAP was related to alteration of the membrane permeability in P. porphyrae. Glucan (dpeaa)DE-He213 Antifungal Protein (dpeaa)DE-He213 Alcaligenes Faecalis (dpeaa)DE-He213 Strain AP77 (dpeaa)DE-He213 Antifungal Mechanism (dpeaa)DE-He213 Kamei, Y. aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 62(2003), 4 vom: 23. Mai, Seite 407-413 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:62 year:2003 number:4 day:23 month:05 pages:407-413 https://dx.doi.org/10.1007/s00253-003-1235-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 62 2003 4 23 05 407-413 |
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10.1007/s00253-003-1235-5 doi (DE-627)SPR002931869 (SPR)s00253-003-1235-5-e DE-627 ger DE-627 rakwb eng Woo, J.-H. verfasserin aut Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp. 2003 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2003 Abstract Previously we reported an antifungal protein specific to Pythium porphyrae, a causative agent of red rot disease afflicting seaweed Porphyra spp. This study was carried out to identify the antifungal mechanism of the antifungal protein to P. porphyrae. When we first examined the effect of an anti-Pythium protein (SAP) on the P. porphyrae cell walls, SAP did not decompose the six structural polysaccharides in Pythium cell walls. However, hyphal growth was significantly inhibited in Pythium cells treated with 50 μg/ml of SAP by MTT assay. Protoplasmic leakage was observed in P. porphyrae hyphae treated with SAP for 1 h, followed by hyphal swelling and disintegration, using SYTOX Green, and SAP permeabilized the membrane of P. porphyrae in a dose-dependent manner. Treating P. porphyrae cells with SAP in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP), a membrane-depolarizing agent, significantly reduced the membrane permeability to SYTOX Green. Moreover, a similar effect was observed when the P. porphyrae cells were treated with SAP in the presence of $ MgCl_{2} $. In contrast, identical treatment in the presence of KCl significantly increased the membrane permeability to SYTOX Green. These results suggested that anti-Pythium mechanism of SAP was related to alteration of the membrane permeability in P. porphyrae. Glucan (dpeaa)DE-He213 Antifungal Protein (dpeaa)DE-He213 Alcaligenes Faecalis (dpeaa)DE-He213 Strain AP77 (dpeaa)DE-He213 Antifungal Mechanism (dpeaa)DE-He213 Kamei, Y. aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 62(2003), 4 vom: 23. Mai, Seite 407-413 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:62 year:2003 number:4 day:23 month:05 pages:407-413 https://dx.doi.org/10.1007/s00253-003-1235-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 62 2003 4 23 05 407-413 |
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10.1007/s00253-003-1235-5 doi (DE-627)SPR002931869 (SPR)s00253-003-1235-5-e DE-627 ger DE-627 rakwb eng Woo, J.-H. verfasserin aut Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp. 2003 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2003 Abstract Previously we reported an antifungal protein specific to Pythium porphyrae, a causative agent of red rot disease afflicting seaweed Porphyra spp. This study was carried out to identify the antifungal mechanism of the antifungal protein to P. porphyrae. When we first examined the effect of an anti-Pythium protein (SAP) on the P. porphyrae cell walls, SAP did not decompose the six structural polysaccharides in Pythium cell walls. However, hyphal growth was significantly inhibited in Pythium cells treated with 50 μg/ml of SAP by MTT assay. Protoplasmic leakage was observed in P. porphyrae hyphae treated with SAP for 1 h, followed by hyphal swelling and disintegration, using SYTOX Green, and SAP permeabilized the membrane of P. porphyrae in a dose-dependent manner. Treating P. porphyrae cells with SAP in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP), a membrane-depolarizing agent, significantly reduced the membrane permeability to SYTOX Green. Moreover, a similar effect was observed when the P. porphyrae cells were treated with SAP in the presence of $ MgCl_{2} $. In contrast, identical treatment in the presence of KCl significantly increased the membrane permeability to SYTOX Green. These results suggested that anti-Pythium mechanism of SAP was related to alteration of the membrane permeability in P. porphyrae. Glucan (dpeaa)DE-He213 Antifungal Protein (dpeaa)DE-He213 Alcaligenes Faecalis (dpeaa)DE-He213 Strain AP77 (dpeaa)DE-He213 Antifungal Mechanism (dpeaa)DE-He213 Kamei, Y. aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 62(2003), 4 vom: 23. Mai, Seite 407-413 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:62 year:2003 number:4 day:23 month:05 pages:407-413 https://dx.doi.org/10.1007/s00253-003-1235-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 62 2003 4 23 05 407-413 |
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10.1007/s00253-003-1235-5 doi (DE-627)SPR002931869 (SPR)s00253-003-1235-5-e DE-627 ger DE-627 rakwb eng Woo, J.-H. verfasserin aut Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp. 2003 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2003 Abstract Previously we reported an antifungal protein specific to Pythium porphyrae, a causative agent of red rot disease afflicting seaweed Porphyra spp. This study was carried out to identify the antifungal mechanism of the antifungal protein to P. porphyrae. When we first examined the effect of an anti-Pythium protein (SAP) on the P. porphyrae cell walls, SAP did not decompose the six structural polysaccharides in Pythium cell walls. However, hyphal growth was significantly inhibited in Pythium cells treated with 50 μg/ml of SAP by MTT assay. Protoplasmic leakage was observed in P. porphyrae hyphae treated with SAP for 1 h, followed by hyphal swelling and disintegration, using SYTOX Green, and SAP permeabilized the membrane of P. porphyrae in a dose-dependent manner. Treating P. porphyrae cells with SAP in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP), a membrane-depolarizing agent, significantly reduced the membrane permeability to SYTOX Green. Moreover, a similar effect was observed when the P. porphyrae cells were treated with SAP in the presence of $ MgCl_{2} $. In contrast, identical treatment in the presence of KCl significantly increased the membrane permeability to SYTOX Green. These results suggested that anti-Pythium mechanism of SAP was related to alteration of the membrane permeability in P. porphyrae. Glucan (dpeaa)DE-He213 Antifungal Protein (dpeaa)DE-He213 Alcaligenes Faecalis (dpeaa)DE-He213 Strain AP77 (dpeaa)DE-He213 Antifungal Mechanism (dpeaa)DE-He213 Kamei, Y. aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 62(2003), 4 vom: 23. Mai, Seite 407-413 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:62 year:2003 number:4 day:23 month:05 pages:407-413 https://dx.doi.org/10.1007/s00253-003-1235-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 62 2003 4 23 05 407-413 |
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Enthalten in Applied microbiology and biotechnology 62(2003), 4 vom: 23. Mai, Seite 407-413 volume:62 year:2003 number:4 day:23 month:05 pages:407-413 |
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Enthalten in Applied microbiology and biotechnology 62(2003), 4 vom: 23. Mai, Seite 407-413 volume:62 year:2003 number:4 day:23 month:05 pages:407-413 |
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Glucan Antifungal Protein Alcaligenes Faecalis Strain AP77 Antifungal Mechanism |
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When we first examined the effect of an anti-Pythium protein (SAP) on the P. porphyrae cell walls, SAP did not decompose the six structural polysaccharides in Pythium cell walls. However, hyphal growth was significantly inhibited in Pythium cells treated with 50 μg/ml of SAP by MTT assay. Protoplasmic leakage was observed in P. porphyrae hyphae treated with SAP for 1 h, followed by hyphal swelling and disintegration, using SYTOX Green, and SAP permeabilized the membrane of P. porphyrae in a dose-dependent manner. Treating P. porphyrae cells with SAP in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP), a membrane-depolarizing agent, significantly reduced the membrane permeability to SYTOX Green. Moreover, a similar effect was observed when the P. porphyrae cells were treated with SAP in the presence of $ MgCl_{2} $. In contrast, identical treatment in the presence of KCl significantly increased the membrane permeability to SYTOX Green. 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Woo, J.-H. |
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Woo, J.-H. misc Glucan misc Antifungal Protein misc Alcaligenes Faecalis misc Strain AP77 misc Antifungal Mechanism Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp. |
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Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp Glucan (dpeaa)DE-He213 Antifungal Protein (dpeaa)DE-He213 Alcaligenes Faecalis (dpeaa)DE-He213 Strain AP77 (dpeaa)DE-He213 Antifungal Mechanism (dpeaa)DE-He213 |
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Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp. |
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Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp |
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antifungal mechanism of an anti-pythium protein (sap) from the marine bacterium streptomyces sp. strain ap77 is specific for pythium porphyrae, a causative agent of red rot disease in porphyra spp |
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Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp. |
| abstract |
Abstract Previously we reported an antifungal protein specific to Pythium porphyrae, a causative agent of red rot disease afflicting seaweed Porphyra spp. This study was carried out to identify the antifungal mechanism of the antifungal protein to P. porphyrae. When we first examined the effect of an anti-Pythium protein (SAP) on the P. porphyrae cell walls, SAP did not decompose the six structural polysaccharides in Pythium cell walls. However, hyphal growth was significantly inhibited in Pythium cells treated with 50 μg/ml of SAP by MTT assay. Protoplasmic leakage was observed in P. porphyrae hyphae treated with SAP for 1 h, followed by hyphal swelling and disintegration, using SYTOX Green, and SAP permeabilized the membrane of P. porphyrae in a dose-dependent manner. Treating P. porphyrae cells with SAP in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP), a membrane-depolarizing agent, significantly reduced the membrane permeability to SYTOX Green. Moreover, a similar effect was observed when the P. porphyrae cells were treated with SAP in the presence of $ MgCl_{2} $. In contrast, identical treatment in the presence of KCl significantly increased the membrane permeability to SYTOX Green. These results suggested that anti-Pythium mechanism of SAP was related to alteration of the membrane permeability in P. porphyrae. © Springer-Verlag 2003 |
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Abstract Previously we reported an antifungal protein specific to Pythium porphyrae, a causative agent of red rot disease afflicting seaweed Porphyra spp. This study was carried out to identify the antifungal mechanism of the antifungal protein to P. porphyrae. When we first examined the effect of an anti-Pythium protein (SAP) on the P. porphyrae cell walls, SAP did not decompose the six structural polysaccharides in Pythium cell walls. However, hyphal growth was significantly inhibited in Pythium cells treated with 50 μg/ml of SAP by MTT assay. Protoplasmic leakage was observed in P. porphyrae hyphae treated with SAP for 1 h, followed by hyphal swelling and disintegration, using SYTOX Green, and SAP permeabilized the membrane of P. porphyrae in a dose-dependent manner. Treating P. porphyrae cells with SAP in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP), a membrane-depolarizing agent, significantly reduced the membrane permeability to SYTOX Green. Moreover, a similar effect was observed when the P. porphyrae cells were treated with SAP in the presence of $ MgCl_{2} $. In contrast, identical treatment in the presence of KCl significantly increased the membrane permeability to SYTOX Green. These results suggested that anti-Pythium mechanism of SAP was related to alteration of the membrane permeability in P. porphyrae. © Springer-Verlag 2003 |
| abstract_unstemmed |
Abstract Previously we reported an antifungal protein specific to Pythium porphyrae, a causative agent of red rot disease afflicting seaweed Porphyra spp. This study was carried out to identify the antifungal mechanism of the antifungal protein to P. porphyrae. When we first examined the effect of an anti-Pythium protein (SAP) on the P. porphyrae cell walls, SAP did not decompose the six structural polysaccharides in Pythium cell walls. However, hyphal growth was significantly inhibited in Pythium cells treated with 50 μg/ml of SAP by MTT assay. Protoplasmic leakage was observed in P. porphyrae hyphae treated with SAP for 1 h, followed by hyphal swelling and disintegration, using SYTOX Green, and SAP permeabilized the membrane of P. porphyrae in a dose-dependent manner. Treating P. porphyrae cells with SAP in the presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP), a membrane-depolarizing agent, significantly reduced the membrane permeability to SYTOX Green. Moreover, a similar effect was observed when the P. porphyrae cells were treated with SAP in the presence of $ MgCl_{2} $. In contrast, identical treatment in the presence of KCl significantly increased the membrane permeability to SYTOX Green. These results suggested that anti-Pythium mechanism of SAP was related to alteration of the membrane permeability in P. porphyrae. © Springer-Verlag 2003 |
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Antifungal mechanism of an anti-Pythium protein (SAP) from the marine bacterium Streptomyces sp. strain AP77 is specific for Pythium porphyrae, a causative agent of red rot disease in Porphyra spp. |
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https://dx.doi.org/10.1007/s00253-003-1235-5 |
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| score |
7.3992643 |