Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae
Abstract Although, classical swine fever virus (CSFV) envelope glycoprotein E2 subunit vaccine has been developed using the baculovirus expression system, the expression of viral antigens in baculovirus-infected insect cells is often ineffective. Therefore, an alternative strategy to the traditional...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Lee, Kwang Sik [verfasserIn] Sohn, Mi Ri [verfasserIn] Kim, Bo Yeon [verfasserIn] Choo, Young Moo [verfasserIn] Woo, Soo Dong [verfasserIn] Yoo, Sung Sik [verfasserIn] Je, Yeon Ho [verfasserIn] Choi, Jae Young [verfasserIn] Roh, Jong Yul [verfasserIn] Koo, Hyun Na [verfasserIn] Jin, Byung Rae [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2011 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Molecular biotechnology - New York, NY : Springer, 1994, 50(2011), 3 vom: 25. Juni, Seite 211-220 |
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| Übergeordnetes Werk: |
volume:50 ; year:2011 ; number:3 ; day:25 ; month:06 ; pages:211-220 |
| Links: |
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| DOI / URN: |
10.1007/s12033-011-9431-5 |
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| Katalog-ID: |
SPR023907932 |
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| 100 | 1 | |a Lee, Kwang Sik |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae |
| 264 | 1 | |c 2011 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 520 | |a Abstract Although, classical swine fever virus (CSFV) envelope glycoprotein E2 subunit vaccine has been developed using the baculovirus expression system, the expression of viral antigens in baculovirus-infected insect cells is often ineffective. Therefore, an alternative strategy to the traditional baculovirus expression system is needed that is more productive and effective. Here, we report a novel strategy for the large-scale production of a CSFV E2 in the larvae of a baculovirus-infected silkworm, Bombyx mori. We constructed a recombinant B. mori nucleopolyhedrovirus (BmNPV) that expressed recombinant polyhedra together with the N-terminal 179 amino acids of CSFV E2 (E2ΔC). BmNPV-E2ΔC-infected silkworm larvae expressed native polyhedrin and approximately 44-kDa fusion protein that was detected using both anti-polyhedrin and anti-CSFV E2 antibodies. Electron and confocal microscopy both demonstrated that the recombinant polyhedra contained both the fusion protein and native polyhedrin were morphologically normal and contained CSFV E2ΔC. The CSFV E2ΔC antigen produced in BmNPV-E2ΔC-infected silkworm larvae reached 0.68 mg/ml of hemolymph and 0.53 mg/larva at 6-days post-infection. Six-week-old female BALB/c mice that were immunized with the E2ΔC protein purified from solubilized recombinant polyhedra elicited CSFV E2 antibodies, which indicated that the CSFV E2ΔC protein from recombinant polyhedra was immunogenic. The virus neutralization test showed that the serum from mice that were treated with E2ΔC protein from recombinant polyhedra contained significant levels of virus neutralization activity. These results demonstrate that this strategy can be used for the large-scale production of CSFV E2 antigen. | ||
| 650 | 4 | |a Classical swine fever virus (CSFV) |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Envelope glycoprotein E2 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a nucleopolyhedrovirus (BmNPV) |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Recombinant polyhedra |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Silkworm |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Vaccine |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Sohn, Mi Ri |e verfasserin |4 aut | |
| 700 | 1 | |a Kim, Bo Yeon |e verfasserin |4 aut | |
| 700 | 1 | |a Choo, Young Moo |e verfasserin |4 aut | |
| 700 | 1 | |a Woo, Soo Dong |e verfasserin |4 aut | |
| 700 | 1 | |a Yoo, Sung Sik |e verfasserin |4 aut | |
| 700 | 1 | |a Je, Yeon Ho |e verfasserin |4 aut | |
| 700 | 1 | |a Choi, Jae Young |e verfasserin |4 aut | |
| 700 | 1 | |a Roh, Jong Yul |e verfasserin |4 aut | |
| 700 | 1 | |a Koo, Hyun Na |e verfasserin |4 aut | |
| 700 | 1 | |a Jin, Byung Rae |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Molecular biotechnology |d New York, NY : Springer, 1994 |g 50(2011), 3 vom: 25. Juni, Seite 211-220 |w (DE-627)343966271 |w (DE-600)2073594-7 |x 1559-0305 |7 nnns |
| 773 | 1 | 8 | |g volume:50 |g year:2011 |g number:3 |g day:25 |g month:06 |g pages:211-220 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1007/s12033-011-9431-5 |z lizenzpflichtig |3 Volltext |
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| 952 | |d 50 |j 2011 |e 3 |b 25 |c 06 |h 211-220 | ||
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2011 |
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2011 |
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10.1007/s12033-011-9431-5 doi (DE-627)SPR023907932 (SPR)s12033-011-9431-5-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.13 bkl Lee, Kwang Sik verfasserin aut Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Although, classical swine fever virus (CSFV) envelope glycoprotein E2 subunit vaccine has been developed using the baculovirus expression system, the expression of viral antigens in baculovirus-infected insect cells is often ineffective. Therefore, an alternative strategy to the traditional baculovirus expression system is needed that is more productive and effective. Here, we report a novel strategy for the large-scale production of a CSFV E2 in the larvae of a baculovirus-infected silkworm, Bombyx mori. We constructed a recombinant B. mori nucleopolyhedrovirus (BmNPV) that expressed recombinant polyhedra together with the N-terminal 179 amino acids of CSFV E2 (E2ΔC). BmNPV-E2ΔC-infected silkworm larvae expressed native polyhedrin and approximately 44-kDa fusion protein that was detected using both anti-polyhedrin and anti-CSFV E2 antibodies. Electron and confocal microscopy both demonstrated that the recombinant polyhedra contained both the fusion protein and native polyhedrin were morphologically normal and contained CSFV E2ΔC. The CSFV E2ΔC antigen produced in BmNPV-E2ΔC-infected silkworm larvae reached 0.68 mg/ml of hemolymph and 0.53 mg/larva at 6-days post-infection. Six-week-old female BALB/c mice that were immunized with the E2ΔC protein purified from solubilized recombinant polyhedra elicited CSFV E2 antibodies, which indicated that the CSFV E2ΔC protein from recombinant polyhedra was immunogenic. The virus neutralization test showed that the serum from mice that were treated with E2ΔC protein from recombinant polyhedra contained significant levels of virus neutralization activity. These results demonstrate that this strategy can be used for the large-scale production of CSFV E2 antigen. Classical swine fever virus (CSFV) (dpeaa)DE-He213 Envelope glycoprotein E2 (dpeaa)DE-He213 nucleopolyhedrovirus (BmNPV) (dpeaa)DE-He213 Recombinant polyhedra (dpeaa)DE-He213 Silkworm (dpeaa)DE-He213 Vaccine (dpeaa)DE-He213 Sohn, Mi Ri verfasserin aut Kim, Bo Yeon verfasserin aut Choo, Young Moo verfasserin aut Woo, Soo Dong verfasserin aut Yoo, Sung Sik verfasserin aut Je, Yeon Ho verfasserin aut Choi, Jae Young verfasserin aut Roh, Jong Yul verfasserin aut Koo, Hyun Na verfasserin aut Jin, Byung Rae verfasserin aut Enthalten in Molecular biotechnology New York, NY : Springer, 1994 50(2011), 3 vom: 25. Juni, Seite 211-220 (DE-627)343966271 (DE-600)2073594-7 1559-0305 nnns volume:50 year:2011 number:3 day:25 month:06 pages:211-220 https://dx.doi.org/10.1007/s12033-011-9431-5 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_65 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_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 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_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.13 ASE AR 50 2011 3 25 06 211-220 |
| spelling |
10.1007/s12033-011-9431-5 doi (DE-627)SPR023907932 (SPR)s12033-011-9431-5-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.13 bkl Lee, Kwang Sik verfasserin aut Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Although, classical swine fever virus (CSFV) envelope glycoprotein E2 subunit vaccine has been developed using the baculovirus expression system, the expression of viral antigens in baculovirus-infected insect cells is often ineffective. Therefore, an alternative strategy to the traditional baculovirus expression system is needed that is more productive and effective. Here, we report a novel strategy for the large-scale production of a CSFV E2 in the larvae of a baculovirus-infected silkworm, Bombyx mori. We constructed a recombinant B. mori nucleopolyhedrovirus (BmNPV) that expressed recombinant polyhedra together with the N-terminal 179 amino acids of CSFV E2 (E2ΔC). BmNPV-E2ΔC-infected silkworm larvae expressed native polyhedrin and approximately 44-kDa fusion protein that was detected using both anti-polyhedrin and anti-CSFV E2 antibodies. Electron and confocal microscopy both demonstrated that the recombinant polyhedra contained both the fusion protein and native polyhedrin were morphologically normal and contained CSFV E2ΔC. The CSFV E2ΔC antigen produced in BmNPV-E2ΔC-infected silkworm larvae reached 0.68 mg/ml of hemolymph and 0.53 mg/larva at 6-days post-infection. Six-week-old female BALB/c mice that were immunized with the E2ΔC protein purified from solubilized recombinant polyhedra elicited CSFV E2 antibodies, which indicated that the CSFV E2ΔC protein from recombinant polyhedra was immunogenic. The virus neutralization test showed that the serum from mice that were treated with E2ΔC protein from recombinant polyhedra contained significant levels of virus neutralization activity. These results demonstrate that this strategy can be used for the large-scale production of CSFV E2 antigen. Classical swine fever virus (CSFV) (dpeaa)DE-He213 Envelope glycoprotein E2 (dpeaa)DE-He213 nucleopolyhedrovirus (BmNPV) (dpeaa)DE-He213 Recombinant polyhedra (dpeaa)DE-He213 Silkworm (dpeaa)DE-He213 Vaccine (dpeaa)DE-He213 Sohn, Mi Ri verfasserin aut Kim, Bo Yeon verfasserin aut Choo, Young Moo verfasserin aut Woo, Soo Dong verfasserin aut Yoo, Sung Sik verfasserin aut Je, Yeon Ho verfasserin aut Choi, Jae Young verfasserin aut Roh, Jong Yul verfasserin aut Koo, Hyun Na verfasserin aut Jin, Byung Rae verfasserin aut Enthalten in Molecular biotechnology New York, NY : Springer, 1994 50(2011), 3 vom: 25. Juni, Seite 211-220 (DE-627)343966271 (DE-600)2073594-7 1559-0305 nnns volume:50 year:2011 number:3 day:25 month:06 pages:211-220 https://dx.doi.org/10.1007/s12033-011-9431-5 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_65 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_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 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_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.13 ASE AR 50 2011 3 25 06 211-220 |
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10.1007/s12033-011-9431-5 doi (DE-627)SPR023907932 (SPR)s12033-011-9431-5-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.13 bkl Lee, Kwang Sik verfasserin aut Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Although, classical swine fever virus (CSFV) envelope glycoprotein E2 subunit vaccine has been developed using the baculovirus expression system, the expression of viral antigens in baculovirus-infected insect cells is often ineffective. Therefore, an alternative strategy to the traditional baculovirus expression system is needed that is more productive and effective. Here, we report a novel strategy for the large-scale production of a CSFV E2 in the larvae of a baculovirus-infected silkworm, Bombyx mori. We constructed a recombinant B. mori nucleopolyhedrovirus (BmNPV) that expressed recombinant polyhedra together with the N-terminal 179 amino acids of CSFV E2 (E2ΔC). BmNPV-E2ΔC-infected silkworm larvae expressed native polyhedrin and approximately 44-kDa fusion protein that was detected using both anti-polyhedrin and anti-CSFV E2 antibodies. Electron and confocal microscopy both demonstrated that the recombinant polyhedra contained both the fusion protein and native polyhedrin were morphologically normal and contained CSFV E2ΔC. The CSFV E2ΔC antigen produced in BmNPV-E2ΔC-infected silkworm larvae reached 0.68 mg/ml of hemolymph and 0.53 mg/larva at 6-days post-infection. Six-week-old female BALB/c mice that were immunized with the E2ΔC protein purified from solubilized recombinant polyhedra elicited CSFV E2 antibodies, which indicated that the CSFV E2ΔC protein from recombinant polyhedra was immunogenic. The virus neutralization test showed that the serum from mice that were treated with E2ΔC protein from recombinant polyhedra contained significant levels of virus neutralization activity. These results demonstrate that this strategy can be used for the large-scale production of CSFV E2 antigen. Classical swine fever virus (CSFV) (dpeaa)DE-He213 Envelope glycoprotein E2 (dpeaa)DE-He213 nucleopolyhedrovirus (BmNPV) (dpeaa)DE-He213 Recombinant polyhedra (dpeaa)DE-He213 Silkworm (dpeaa)DE-He213 Vaccine (dpeaa)DE-He213 Sohn, Mi Ri verfasserin aut Kim, Bo Yeon verfasserin aut Choo, Young Moo verfasserin aut Woo, Soo Dong verfasserin aut Yoo, Sung Sik verfasserin aut Je, Yeon Ho verfasserin aut Choi, Jae Young verfasserin aut Roh, Jong Yul verfasserin aut Koo, Hyun Na verfasserin aut Jin, Byung Rae verfasserin aut Enthalten in Molecular biotechnology New York, NY : Springer, 1994 50(2011), 3 vom: 25. Juni, Seite 211-220 (DE-627)343966271 (DE-600)2073594-7 1559-0305 nnns volume:50 year:2011 number:3 day:25 month:06 pages:211-220 https://dx.doi.org/10.1007/s12033-011-9431-5 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_65 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_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 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_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.13 ASE AR 50 2011 3 25 06 211-220 |
| allfieldsGer |
10.1007/s12033-011-9431-5 doi (DE-627)SPR023907932 (SPR)s12033-011-9431-5-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.13 bkl Lee, Kwang Sik verfasserin aut Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Although, classical swine fever virus (CSFV) envelope glycoprotein E2 subunit vaccine has been developed using the baculovirus expression system, the expression of viral antigens in baculovirus-infected insect cells is often ineffective. Therefore, an alternative strategy to the traditional baculovirus expression system is needed that is more productive and effective. Here, we report a novel strategy for the large-scale production of a CSFV E2 in the larvae of a baculovirus-infected silkworm, Bombyx mori. We constructed a recombinant B. mori nucleopolyhedrovirus (BmNPV) that expressed recombinant polyhedra together with the N-terminal 179 amino acids of CSFV E2 (E2ΔC). BmNPV-E2ΔC-infected silkworm larvae expressed native polyhedrin and approximately 44-kDa fusion protein that was detected using both anti-polyhedrin and anti-CSFV E2 antibodies. Electron and confocal microscopy both demonstrated that the recombinant polyhedra contained both the fusion protein and native polyhedrin were morphologically normal and contained CSFV E2ΔC. The CSFV E2ΔC antigen produced in BmNPV-E2ΔC-infected silkworm larvae reached 0.68 mg/ml of hemolymph and 0.53 mg/larva at 6-days post-infection. Six-week-old female BALB/c mice that were immunized with the E2ΔC protein purified from solubilized recombinant polyhedra elicited CSFV E2 antibodies, which indicated that the CSFV E2ΔC protein from recombinant polyhedra was immunogenic. The virus neutralization test showed that the serum from mice that were treated with E2ΔC protein from recombinant polyhedra contained significant levels of virus neutralization activity. These results demonstrate that this strategy can be used for the large-scale production of CSFV E2 antigen. Classical swine fever virus (CSFV) (dpeaa)DE-He213 Envelope glycoprotein E2 (dpeaa)DE-He213 nucleopolyhedrovirus (BmNPV) (dpeaa)DE-He213 Recombinant polyhedra (dpeaa)DE-He213 Silkworm (dpeaa)DE-He213 Vaccine (dpeaa)DE-He213 Sohn, Mi Ri verfasserin aut Kim, Bo Yeon verfasserin aut Choo, Young Moo verfasserin aut Woo, Soo Dong verfasserin aut Yoo, Sung Sik verfasserin aut Je, Yeon Ho verfasserin aut Choi, Jae Young verfasserin aut Roh, Jong Yul verfasserin aut Koo, Hyun Na verfasserin aut Jin, Byung Rae verfasserin aut Enthalten in Molecular biotechnology New York, NY : Springer, 1994 50(2011), 3 vom: 25. Juni, Seite 211-220 (DE-627)343966271 (DE-600)2073594-7 1559-0305 nnns volume:50 year:2011 number:3 day:25 month:06 pages:211-220 https://dx.doi.org/10.1007/s12033-011-9431-5 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_65 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_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 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_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.13 ASE AR 50 2011 3 25 06 211-220 |
| allfieldsSound |
10.1007/s12033-011-9431-5 doi (DE-627)SPR023907932 (SPR)s12033-011-9431-5-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.13 bkl Lee, Kwang Sik verfasserin aut Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Although, classical swine fever virus (CSFV) envelope glycoprotein E2 subunit vaccine has been developed using the baculovirus expression system, the expression of viral antigens in baculovirus-infected insect cells is often ineffective. Therefore, an alternative strategy to the traditional baculovirus expression system is needed that is more productive and effective. Here, we report a novel strategy for the large-scale production of a CSFV E2 in the larvae of a baculovirus-infected silkworm, Bombyx mori. We constructed a recombinant B. mori nucleopolyhedrovirus (BmNPV) that expressed recombinant polyhedra together with the N-terminal 179 amino acids of CSFV E2 (E2ΔC). BmNPV-E2ΔC-infected silkworm larvae expressed native polyhedrin and approximately 44-kDa fusion protein that was detected using both anti-polyhedrin and anti-CSFV E2 antibodies. Electron and confocal microscopy both demonstrated that the recombinant polyhedra contained both the fusion protein and native polyhedrin were morphologically normal and contained CSFV E2ΔC. The CSFV E2ΔC antigen produced in BmNPV-E2ΔC-infected silkworm larvae reached 0.68 mg/ml of hemolymph and 0.53 mg/larva at 6-days post-infection. Six-week-old female BALB/c mice that were immunized with the E2ΔC protein purified from solubilized recombinant polyhedra elicited CSFV E2 antibodies, which indicated that the CSFV E2ΔC protein from recombinant polyhedra was immunogenic. The virus neutralization test showed that the serum from mice that were treated with E2ΔC protein from recombinant polyhedra contained significant levels of virus neutralization activity. These results demonstrate that this strategy can be used for the large-scale production of CSFV E2 antigen. Classical swine fever virus (CSFV) (dpeaa)DE-He213 Envelope glycoprotein E2 (dpeaa)DE-He213 nucleopolyhedrovirus (BmNPV) (dpeaa)DE-He213 Recombinant polyhedra (dpeaa)DE-He213 Silkworm (dpeaa)DE-He213 Vaccine (dpeaa)DE-He213 Sohn, Mi Ri verfasserin aut Kim, Bo Yeon verfasserin aut Choo, Young Moo verfasserin aut Woo, Soo Dong verfasserin aut Yoo, Sung Sik verfasserin aut Je, Yeon Ho verfasserin aut Choi, Jae Young verfasserin aut Roh, Jong Yul verfasserin aut Koo, Hyun Na verfasserin aut Jin, Byung Rae verfasserin aut Enthalten in Molecular biotechnology New York, NY : Springer, 1994 50(2011), 3 vom: 25. Juni, Seite 211-220 (DE-627)343966271 (DE-600)2073594-7 1559-0305 nnns volume:50 year:2011 number:3 day:25 month:06 pages:211-220 https://dx.doi.org/10.1007/s12033-011-9431-5 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_65 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_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 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_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.13 ASE AR 50 2011 3 25 06 211-220 |
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Enthalten in Molecular biotechnology 50(2011), 3 vom: 25. Juni, Seite 211-220 volume:50 year:2011 number:3 day:25 month:06 pages:211-220 |
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Enthalten in Molecular biotechnology 50(2011), 3 vom: 25. Juni, Seite 211-220 volume:50 year:2011 number:3 day:25 month:06 pages:211-220 |
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Classical swine fever virus (CSFV) Envelope glycoprotein E2 nucleopolyhedrovirus (BmNPV) Recombinant polyhedra Silkworm Vaccine |
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Molecular biotechnology |
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Lee, Kwang Sik @@aut@@ Sohn, Mi Ri @@aut@@ Kim, Bo Yeon @@aut@@ Choo, Young Moo @@aut@@ Woo, Soo Dong @@aut@@ Yoo, Sung Sik @@aut@@ Je, Yeon Ho @@aut@@ Choi, Jae Young @@aut@@ Roh, Jong Yul @@aut@@ Koo, Hyun Na @@aut@@ Jin, Byung Rae @@aut@@ |
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2011-06-25T00:00:00Z |
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|
| author |
Lee, Kwang Sik |
| spellingShingle |
Lee, Kwang Sik ddc 570 bkl 58.30 bkl 42.13 misc Classical swine fever virus (CSFV) misc Envelope glycoprotein E2 misc nucleopolyhedrovirus (BmNPV) misc Recombinant polyhedra misc Silkworm misc Vaccine Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae |
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1559-0305 |
| topic_title |
570 ASE 58.30 bkl 42.13 bkl Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae Classical swine fever virus (CSFV) (dpeaa)DE-He213 Envelope glycoprotein E2 (dpeaa)DE-He213 nucleopolyhedrovirus (BmNPV) (dpeaa)DE-He213 Recombinant polyhedra (dpeaa)DE-He213 Silkworm (dpeaa)DE-He213 Vaccine (dpeaa)DE-He213 |
| topic |
ddc 570 bkl 58.30 bkl 42.13 misc Classical swine fever virus (CSFV) misc Envelope glycoprotein E2 misc nucleopolyhedrovirus (BmNPV) misc Recombinant polyhedra misc Silkworm misc Vaccine |
| topic_unstemmed |
ddc 570 bkl 58.30 bkl 42.13 misc Classical swine fever virus (CSFV) misc Envelope glycoprotein E2 misc nucleopolyhedrovirus (BmNPV) misc Recombinant polyhedra misc Silkworm misc Vaccine |
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ddc 570 bkl 58.30 bkl 42.13 misc Classical swine fever virus (CSFV) misc Envelope glycoprotein E2 misc nucleopolyhedrovirus (BmNPV) misc Recombinant polyhedra misc Silkworm misc Vaccine |
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570 - Life sciences; biology |
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Molecular biotechnology |
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| title |
Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae |
| ctrlnum |
(DE-627)SPR023907932 (SPR)s12033-011-9431-5-e |
| title_full |
Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae |
| author_sort |
Lee, Kwang Sik |
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Molecular biotechnology |
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Molecular biotechnology |
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eng |
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500 - Science |
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2011 |
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Lee, Kwang Sik Sohn, Mi Ri Kim, Bo Yeon Choo, Young Moo Woo, Soo Dong Yoo, Sung Sik Je, Yeon Ho Choi, Jae Young Roh, Jong Yul Koo, Hyun Na Jin, Byung Rae |
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Elektronische Aufsätze |
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Lee, Kwang Sik |
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10.1007/s12033-011-9431-5 |
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570 |
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verfasserin |
| title_sort |
production of classical swine fever virus envelope glycoprotein e2 as recombinant polyhedra in baculovirus-infected silkworm larvae |
| title_auth |
Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae |
| abstract |
Abstract Although, classical swine fever virus (CSFV) envelope glycoprotein E2 subunit vaccine has been developed using the baculovirus expression system, the expression of viral antigens in baculovirus-infected insect cells is often ineffective. Therefore, an alternative strategy to the traditional baculovirus expression system is needed that is more productive and effective. Here, we report a novel strategy for the large-scale production of a CSFV E2 in the larvae of a baculovirus-infected silkworm, Bombyx mori. We constructed a recombinant B. mori nucleopolyhedrovirus (BmNPV) that expressed recombinant polyhedra together with the N-terminal 179 amino acids of CSFV E2 (E2ΔC). BmNPV-E2ΔC-infected silkworm larvae expressed native polyhedrin and approximately 44-kDa fusion protein that was detected using both anti-polyhedrin and anti-CSFV E2 antibodies. Electron and confocal microscopy both demonstrated that the recombinant polyhedra contained both the fusion protein and native polyhedrin were morphologically normal and contained CSFV E2ΔC. The CSFV E2ΔC antigen produced in BmNPV-E2ΔC-infected silkworm larvae reached 0.68 mg/ml of hemolymph and 0.53 mg/larva at 6-days post-infection. Six-week-old female BALB/c mice that were immunized with the E2ΔC protein purified from solubilized recombinant polyhedra elicited CSFV E2 antibodies, which indicated that the CSFV E2ΔC protein from recombinant polyhedra was immunogenic. The virus neutralization test showed that the serum from mice that were treated with E2ΔC protein from recombinant polyhedra contained significant levels of virus neutralization activity. These results demonstrate that this strategy can be used for the large-scale production of CSFV E2 antigen. |
| abstractGer |
Abstract Although, classical swine fever virus (CSFV) envelope glycoprotein E2 subunit vaccine has been developed using the baculovirus expression system, the expression of viral antigens in baculovirus-infected insect cells is often ineffective. Therefore, an alternative strategy to the traditional baculovirus expression system is needed that is more productive and effective. Here, we report a novel strategy for the large-scale production of a CSFV E2 in the larvae of a baculovirus-infected silkworm, Bombyx mori. We constructed a recombinant B. mori nucleopolyhedrovirus (BmNPV) that expressed recombinant polyhedra together with the N-terminal 179 amino acids of CSFV E2 (E2ΔC). BmNPV-E2ΔC-infected silkworm larvae expressed native polyhedrin and approximately 44-kDa fusion protein that was detected using both anti-polyhedrin and anti-CSFV E2 antibodies. Electron and confocal microscopy both demonstrated that the recombinant polyhedra contained both the fusion protein and native polyhedrin were morphologically normal and contained CSFV E2ΔC. The CSFV E2ΔC antigen produced in BmNPV-E2ΔC-infected silkworm larvae reached 0.68 mg/ml of hemolymph and 0.53 mg/larva at 6-days post-infection. Six-week-old female BALB/c mice that were immunized with the E2ΔC protein purified from solubilized recombinant polyhedra elicited CSFV E2 antibodies, which indicated that the CSFV E2ΔC protein from recombinant polyhedra was immunogenic. The virus neutralization test showed that the serum from mice that were treated with E2ΔC protein from recombinant polyhedra contained significant levels of virus neutralization activity. These results demonstrate that this strategy can be used for the large-scale production of CSFV E2 antigen. |
| abstract_unstemmed |
Abstract Although, classical swine fever virus (CSFV) envelope glycoprotein E2 subunit vaccine has been developed using the baculovirus expression system, the expression of viral antigens in baculovirus-infected insect cells is often ineffective. Therefore, an alternative strategy to the traditional baculovirus expression system is needed that is more productive and effective. Here, we report a novel strategy for the large-scale production of a CSFV E2 in the larvae of a baculovirus-infected silkworm, Bombyx mori. We constructed a recombinant B. mori nucleopolyhedrovirus (BmNPV) that expressed recombinant polyhedra together with the N-terminal 179 amino acids of CSFV E2 (E2ΔC). BmNPV-E2ΔC-infected silkworm larvae expressed native polyhedrin and approximately 44-kDa fusion protein that was detected using both anti-polyhedrin and anti-CSFV E2 antibodies. Electron and confocal microscopy both demonstrated that the recombinant polyhedra contained both the fusion protein and native polyhedrin were morphologically normal and contained CSFV E2ΔC. The CSFV E2ΔC antigen produced in BmNPV-E2ΔC-infected silkworm larvae reached 0.68 mg/ml of hemolymph and 0.53 mg/larva at 6-days post-infection. Six-week-old female BALB/c mice that were immunized with the E2ΔC protein purified from solubilized recombinant polyhedra elicited CSFV E2 antibodies, which indicated that the CSFV E2ΔC protein from recombinant polyhedra was immunogenic. The virus neutralization test showed that the serum from mice that were treated with E2ΔC protein from recombinant polyhedra contained significant levels of virus neutralization activity. These results demonstrate that this strategy can be used for the large-scale production of CSFV E2 antigen. |
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| title_short |
Production of Classical Swine Fever Virus Envelope Glycoprotein E2 as Recombinant Polyhedra in Baculovirus-Infected Silkworm Larvae |
| url |
https://dx.doi.org/10.1007/s12033-011-9431-5 |
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| author2 |
Sohn, Mi Ri Kim, Bo Yeon Choo, Young Moo Woo, Soo Dong Yoo, Sung Sik Je, Yeon Ho Choi, Jae Young Roh, Jong Yul Koo, Hyun Na Jin, Byung Rae |
| author2Str |
Sohn, Mi Ri Kim, Bo Yeon Choo, Young Moo Woo, Soo Dong Yoo, Sung Sik Je, Yeon Ho Choi, Jae Young Roh, Jong Yul Koo, Hyun Na Jin, Byung Rae |
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| doi_str |
10.1007/s12033-011-9431-5 |
| up_date |
2024-07-03T22:15:11.863Z |
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| score |
7.400589 |