The role of $ F_{1} $ ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei
Background Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral l...
Ausführliche Beschreibung
Autor*in: |
Liang, Yan [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2010 |
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Schlagwörter: |
White Spot Syndrome Virus Infection |
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Anmerkung: |
© Liang et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( |
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Übergeordnetes Werk: |
Enthalten in: Virology journal - London : BioMed Central, 2004, 7(2010), 1 vom: 30. Juni |
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Übergeordnetes Werk: |
volume:7 ; year:2010 ; number:1 ; day:30 ; month:06 |
Links: |
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DOI / URN: |
10.1186/1743-422X-7-144 |
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Katalog-ID: |
SPR029242282 |
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520 | |a Background Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV). Results Two proteins were evident by using a virus overlay protein binding assay (VOPBA) with WSSV. A protein with molecular weight 53 kDa, named BP53, was analyzed in this study, which was homologous with the $ F_{1} $-ATP synthase beta subunit by mass spectrometry analysis. Rapid amplification of cDNA ends (RACE) PCR was performed to identify the full-length cDNA of the bp53 gene. The resulting full-length gene consisted of 1836 bp, encoding 525 amino acids with a calculated molecular mass of 55.98 kDa. The deduced amino acid sequence contained three conserved domains of the $ F_{1} $-ATP synthase beta subunit. BP53 was therefore designated the $ F_{1} $-ATP synthase beta subunit of L. vannamei. The binding of WSSV to BP53 were also confirmed by competitive ELISA binding assay and co-immunoprecipitation on magnetic beads. To investigate the function of BP53 in WSSV infection, it was mixed with WSSV before the mixture was injected intramuscularly into shrimp. The resulting mortality curves showed that recombinant (r) BP53 could attenuate WSSV infection. Conclusions The results revealed that BP53 is involved in WSSV infection. Here is the first time showed the role of shrimp $ F_{1} $-ATP synthase beta subunit in WSSV infection. | ||
650 | 4 | |a White Spot Syndrome Virus |7 (dpeaa)DE-He213 | |
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700 | 1 | |a Cheng, Jun-Jun |4 aut | |
700 | 1 | |a Yang, Bing |4 aut | |
700 | 1 | |a Huang, Jie |4 aut | |
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10.1186/1743-422X-7-144 doi (DE-627)SPR029242282 (SPR)1743-422X-7-144-e DE-627 ger DE-627 rakwb eng Liang, Yan verfasserin aut The role of $ F_{1} $ ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Liang et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV). Results Two proteins were evident by using a virus overlay protein binding assay (VOPBA) with WSSV. A protein with molecular weight 53 kDa, named BP53, was analyzed in this study, which was homologous with the $ F_{1} $-ATP synthase beta subunit by mass spectrometry analysis. Rapid amplification of cDNA ends (RACE) PCR was performed to identify the full-length cDNA of the bp53 gene. The resulting full-length gene consisted of 1836 bp, encoding 525 amino acids with a calculated molecular mass of 55.98 kDa. The deduced amino acid sequence contained three conserved domains of the $ F_{1} $-ATP synthase beta subunit. BP53 was therefore designated the $ F_{1} $-ATP synthase beta subunit of L. vannamei. The binding of WSSV to BP53 were also confirmed by competitive ELISA binding assay and co-immunoprecipitation on magnetic beads. To investigate the function of BP53 in WSSV infection, it was mixed with WSSV before the mixture was injected intramuscularly into shrimp. The resulting mortality curves showed that recombinant (r) BP53 could attenuate WSSV infection. Conclusions The results revealed that BP53 is involved in WSSV infection. Here is the first time showed the role of shrimp $ F_{1} $-ATP synthase beta subunit in WSSV infection. White Spot Syndrome Virus (dpeaa)DE-He213 White Spot Syndrome Virus Infection (dpeaa)DE-He213 Pacifastacus Leniusculus (dpeaa)DE-He213 White Spot Syndrome Virus Challenge (dpeaa)DE-He213 Virus Overlay Protein Binding Assay (dpeaa)DE-He213 Cheng, Jun-Jun aut Yang, Bing aut Huang, Jie aut Enthalten in Virology journal London : BioMed Central, 2004 7(2010), 1 vom: 30. Juni (DE-627)394165004 (DE-600)2160640-7 1743-422X nnns volume:7 year:2010 number:1 day:30 month:06 https://dx.doi.org/10.1186/1743-422X-7-144 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_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2010 1 30 06 |
spelling |
10.1186/1743-422X-7-144 doi (DE-627)SPR029242282 (SPR)1743-422X-7-144-e DE-627 ger DE-627 rakwb eng Liang, Yan verfasserin aut The role of $ F_{1} $ ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Liang et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV). Results Two proteins were evident by using a virus overlay protein binding assay (VOPBA) with WSSV. A protein with molecular weight 53 kDa, named BP53, was analyzed in this study, which was homologous with the $ F_{1} $-ATP synthase beta subunit by mass spectrometry analysis. Rapid amplification of cDNA ends (RACE) PCR was performed to identify the full-length cDNA of the bp53 gene. The resulting full-length gene consisted of 1836 bp, encoding 525 amino acids with a calculated molecular mass of 55.98 kDa. The deduced amino acid sequence contained three conserved domains of the $ F_{1} $-ATP synthase beta subunit. BP53 was therefore designated the $ F_{1} $-ATP synthase beta subunit of L. vannamei. The binding of WSSV to BP53 were also confirmed by competitive ELISA binding assay and co-immunoprecipitation on magnetic beads. To investigate the function of BP53 in WSSV infection, it was mixed with WSSV before the mixture was injected intramuscularly into shrimp. The resulting mortality curves showed that recombinant (r) BP53 could attenuate WSSV infection. Conclusions The results revealed that BP53 is involved in WSSV infection. Here is the first time showed the role of shrimp $ F_{1} $-ATP synthase beta subunit in WSSV infection. White Spot Syndrome Virus (dpeaa)DE-He213 White Spot Syndrome Virus Infection (dpeaa)DE-He213 Pacifastacus Leniusculus (dpeaa)DE-He213 White Spot Syndrome Virus Challenge (dpeaa)DE-He213 Virus Overlay Protein Binding Assay (dpeaa)DE-He213 Cheng, Jun-Jun aut Yang, Bing aut Huang, Jie aut Enthalten in Virology journal London : BioMed Central, 2004 7(2010), 1 vom: 30. Juni (DE-627)394165004 (DE-600)2160640-7 1743-422X nnns volume:7 year:2010 number:1 day:30 month:06 https://dx.doi.org/10.1186/1743-422X-7-144 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_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2010 1 30 06 |
allfields_unstemmed |
10.1186/1743-422X-7-144 doi (DE-627)SPR029242282 (SPR)1743-422X-7-144-e DE-627 ger DE-627 rakwb eng Liang, Yan verfasserin aut The role of $ F_{1} $ ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Liang et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV). Results Two proteins were evident by using a virus overlay protein binding assay (VOPBA) with WSSV. A protein with molecular weight 53 kDa, named BP53, was analyzed in this study, which was homologous with the $ F_{1} $-ATP synthase beta subunit by mass spectrometry analysis. Rapid amplification of cDNA ends (RACE) PCR was performed to identify the full-length cDNA of the bp53 gene. The resulting full-length gene consisted of 1836 bp, encoding 525 amino acids with a calculated molecular mass of 55.98 kDa. The deduced amino acid sequence contained three conserved domains of the $ F_{1} $-ATP synthase beta subunit. BP53 was therefore designated the $ F_{1} $-ATP synthase beta subunit of L. vannamei. The binding of WSSV to BP53 were also confirmed by competitive ELISA binding assay and co-immunoprecipitation on magnetic beads. To investigate the function of BP53 in WSSV infection, it was mixed with WSSV before the mixture was injected intramuscularly into shrimp. The resulting mortality curves showed that recombinant (r) BP53 could attenuate WSSV infection. Conclusions The results revealed that BP53 is involved in WSSV infection. Here is the first time showed the role of shrimp $ F_{1} $-ATP synthase beta subunit in WSSV infection. White Spot Syndrome Virus (dpeaa)DE-He213 White Spot Syndrome Virus Infection (dpeaa)DE-He213 Pacifastacus Leniusculus (dpeaa)DE-He213 White Spot Syndrome Virus Challenge (dpeaa)DE-He213 Virus Overlay Protein Binding Assay (dpeaa)DE-He213 Cheng, Jun-Jun aut Yang, Bing aut Huang, Jie aut Enthalten in Virology journal London : BioMed Central, 2004 7(2010), 1 vom: 30. Juni (DE-627)394165004 (DE-600)2160640-7 1743-422X nnns volume:7 year:2010 number:1 day:30 month:06 https://dx.doi.org/10.1186/1743-422X-7-144 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_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2010 1 30 06 |
allfieldsGer |
10.1186/1743-422X-7-144 doi (DE-627)SPR029242282 (SPR)1743-422X-7-144-e DE-627 ger DE-627 rakwb eng Liang, Yan verfasserin aut The role of $ F_{1} $ ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Liang et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV). Results Two proteins were evident by using a virus overlay protein binding assay (VOPBA) with WSSV. A protein with molecular weight 53 kDa, named BP53, was analyzed in this study, which was homologous with the $ F_{1} $-ATP synthase beta subunit by mass spectrometry analysis. Rapid amplification of cDNA ends (RACE) PCR was performed to identify the full-length cDNA of the bp53 gene. The resulting full-length gene consisted of 1836 bp, encoding 525 amino acids with a calculated molecular mass of 55.98 kDa. The deduced amino acid sequence contained three conserved domains of the $ F_{1} $-ATP synthase beta subunit. BP53 was therefore designated the $ F_{1} $-ATP synthase beta subunit of L. vannamei. The binding of WSSV to BP53 were also confirmed by competitive ELISA binding assay and co-immunoprecipitation on magnetic beads. To investigate the function of BP53 in WSSV infection, it was mixed with WSSV before the mixture was injected intramuscularly into shrimp. The resulting mortality curves showed that recombinant (r) BP53 could attenuate WSSV infection. Conclusions The results revealed that BP53 is involved in WSSV infection. Here is the first time showed the role of shrimp $ F_{1} $-ATP synthase beta subunit in WSSV infection. White Spot Syndrome Virus (dpeaa)DE-He213 White Spot Syndrome Virus Infection (dpeaa)DE-He213 Pacifastacus Leniusculus (dpeaa)DE-He213 White Spot Syndrome Virus Challenge (dpeaa)DE-He213 Virus Overlay Protein Binding Assay (dpeaa)DE-He213 Cheng, Jun-Jun aut Yang, Bing aut Huang, Jie aut Enthalten in Virology journal London : BioMed Central, 2004 7(2010), 1 vom: 30. Juni (DE-627)394165004 (DE-600)2160640-7 1743-422X nnns volume:7 year:2010 number:1 day:30 month:06 https://dx.doi.org/10.1186/1743-422X-7-144 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_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2010 1 30 06 |
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10.1186/1743-422X-7-144 doi (DE-627)SPR029242282 (SPR)1743-422X-7-144-e DE-627 ger DE-627 rakwb eng Liang, Yan verfasserin aut The role of $ F_{1} $ ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei 2010 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Liang et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV). Results Two proteins were evident by using a virus overlay protein binding assay (VOPBA) with WSSV. A protein with molecular weight 53 kDa, named BP53, was analyzed in this study, which was homologous with the $ F_{1} $-ATP synthase beta subunit by mass spectrometry analysis. Rapid amplification of cDNA ends (RACE) PCR was performed to identify the full-length cDNA of the bp53 gene. The resulting full-length gene consisted of 1836 bp, encoding 525 amino acids with a calculated molecular mass of 55.98 kDa. The deduced amino acid sequence contained three conserved domains of the $ F_{1} $-ATP synthase beta subunit. BP53 was therefore designated the $ F_{1} $-ATP synthase beta subunit of L. vannamei. The binding of WSSV to BP53 were also confirmed by competitive ELISA binding assay and co-immunoprecipitation on magnetic beads. To investigate the function of BP53 in WSSV infection, it was mixed with WSSV before the mixture was injected intramuscularly into shrimp. The resulting mortality curves showed that recombinant (r) BP53 could attenuate WSSV infection. Conclusions The results revealed that BP53 is involved in WSSV infection. Here is the first time showed the role of shrimp $ F_{1} $-ATP synthase beta subunit in WSSV infection. White Spot Syndrome Virus (dpeaa)DE-He213 White Spot Syndrome Virus Infection (dpeaa)DE-He213 Pacifastacus Leniusculus (dpeaa)DE-He213 White Spot Syndrome Virus Challenge (dpeaa)DE-He213 Virus Overlay Protein Binding Assay (dpeaa)DE-He213 Cheng, Jun-Jun aut Yang, Bing aut Huang, Jie aut Enthalten in Virology journal London : BioMed Central, 2004 7(2010), 1 vom: 30. Juni (DE-627)394165004 (DE-600)2160640-7 1743-422X nnns volume:7 year:2010 number:1 day:30 month:06 https://dx.doi.org/10.1186/1743-422X-7-144 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_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2010 1 30 06 |
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The role of $ F_{1} $ ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei White Spot Syndrome Virus (dpeaa)DE-He213 White Spot Syndrome Virus Infection (dpeaa)DE-He213 Pacifastacus Leniusculus (dpeaa)DE-He213 White Spot Syndrome Virus Challenge (dpeaa)DE-He213 Virus Overlay Protein Binding Assay (dpeaa)DE-He213 |
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Liang, Yan |
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10.1186/1743-422X-7-144 |
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role of $ f_{1} $ atp synthase beta subunit in wssv infection in the shrimp, litopenaeus vannamei |
title_auth |
The role of $ F_{1} $ ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei |
abstract |
Background Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV). Results Two proteins were evident by using a virus overlay protein binding assay (VOPBA) with WSSV. A protein with molecular weight 53 kDa, named BP53, was analyzed in this study, which was homologous with the $ F_{1} $-ATP synthase beta subunit by mass spectrometry analysis. Rapid amplification of cDNA ends (RACE) PCR was performed to identify the full-length cDNA of the bp53 gene. The resulting full-length gene consisted of 1836 bp, encoding 525 amino acids with a calculated molecular mass of 55.98 kDa. The deduced amino acid sequence contained three conserved domains of the $ F_{1} $-ATP synthase beta subunit. BP53 was therefore designated the $ F_{1} $-ATP synthase beta subunit of L. vannamei. The binding of WSSV to BP53 were also confirmed by competitive ELISA binding assay and co-immunoprecipitation on magnetic beads. To investigate the function of BP53 in WSSV infection, it was mixed with WSSV before the mixture was injected intramuscularly into shrimp. The resulting mortality curves showed that recombinant (r) BP53 could attenuate WSSV infection. Conclusions The results revealed that BP53 is involved in WSSV infection. Here is the first time showed the role of shrimp $ F_{1} $-ATP synthase beta subunit in WSSV infection. © Liang et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( |
abstractGer |
Background Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV). Results Two proteins were evident by using a virus overlay protein binding assay (VOPBA) with WSSV. A protein with molecular weight 53 kDa, named BP53, was analyzed in this study, which was homologous with the $ F_{1} $-ATP synthase beta subunit by mass spectrometry analysis. Rapid amplification of cDNA ends (RACE) PCR was performed to identify the full-length cDNA of the bp53 gene. The resulting full-length gene consisted of 1836 bp, encoding 525 amino acids with a calculated molecular mass of 55.98 kDa. The deduced amino acid sequence contained three conserved domains of the $ F_{1} $-ATP synthase beta subunit. BP53 was therefore designated the $ F_{1} $-ATP synthase beta subunit of L. vannamei. The binding of WSSV to BP53 were also confirmed by competitive ELISA binding assay and co-immunoprecipitation on magnetic beads. To investigate the function of BP53 in WSSV infection, it was mixed with WSSV before the mixture was injected intramuscularly into shrimp. The resulting mortality curves showed that recombinant (r) BP53 could attenuate WSSV infection. Conclusions The results revealed that BP53 is involved in WSSV infection. Here is the first time showed the role of shrimp $ F_{1} $-ATP synthase beta subunit in WSSV infection. © Liang et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( |
abstract_unstemmed |
Background Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV). Results Two proteins were evident by using a virus overlay protein binding assay (VOPBA) with WSSV. A protein with molecular weight 53 kDa, named BP53, was analyzed in this study, which was homologous with the $ F_{1} $-ATP synthase beta subunit by mass spectrometry analysis. Rapid amplification of cDNA ends (RACE) PCR was performed to identify the full-length cDNA of the bp53 gene. The resulting full-length gene consisted of 1836 bp, encoding 525 amino acids with a calculated molecular mass of 55.98 kDa. The deduced amino acid sequence contained three conserved domains of the $ F_{1} $-ATP synthase beta subunit. BP53 was therefore designated the $ F_{1} $-ATP synthase beta subunit of L. vannamei. The binding of WSSV to BP53 were also confirmed by competitive ELISA binding assay and co-immunoprecipitation on magnetic beads. To investigate the function of BP53 in WSSV infection, it was mixed with WSSV before the mixture was injected intramuscularly into shrimp. The resulting mortality curves showed that recombinant (r) BP53 could attenuate WSSV infection. Conclusions The results revealed that BP53 is involved in WSSV infection. Here is the first time showed the role of shrimp $ F_{1} $-ATP synthase beta subunit in WSSV infection. © Liang et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( |
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The role of $ F_{1} $ ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei |
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