Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts

Lumazine synthase from Brucella spp. (BLS) is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity.The inner core domain (VP8d) of VP8 spike protein from bovine rotavirus (BRV) is respons...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Edgardo Federico Alfano [verfasserIn] Ezequiel Matías Lentz [verfasserIn] Demian eBellido [verfasserIn] María José Dus Santos [verfasserIn] Fernando Alberto Goldbaum [verfasserIn] Andrés eWigdorovitz [verfasserIn] Fernando Félix Bravo-Almonacid [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2015

Schlagwörter:	Tobacco Vaccine IgY Bovine rotavirus BLS VP8

Übergeordnetes Werk:	In: Frontiers in Plant Science - Frontiers Media S.A., 2011, 6(2015)
Übergeordnetes Werk:	volume:6 ; year:2015

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fpls.2015.01170

Katalog-ID:	DOAJ015899586

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520			\|a Lumazine synthase from Brucella spp. (BLS) is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity.The inner core domain (VP8d) of VP8 spike protein from bovine rotavirus (BRV) is responsible for viral adhesion to sialic acid residues and infection. It also displays neutralizing epitopes, making it a good candidate for vaccination.In this work, the BLS scaffold was assessed for the first time in plants for recombinant vaccine development by N-terminally fusing BLS to VP8d and expressing the resulting fusion (BLSVP8d) in tobacco chloroplasts. Transplastomic plants were obtained and characterized by Southern, northern and western blot. BLSVP8d was highly expressed, representing 40% of total soluble protein (TSP) (4.85 mg/g fresh tissue). BLSVP8d remained soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature. Soluble protein extracts from fresh and lyophilized leaves were able to induce specific neutralizing IgY antibodies in a laying hen model. This work presents BLS as an interesting platform for highly immunogenic injectable, or even oral, subunit vaccines. Lyophilization of transplastomic leaves expressing stable antigenic fusions to BLS would further reduce costs and simplify downstream processing, purification and storage, allowing for more practical vaccines.
650		4	\|a Tobacco
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650		4	\|a Bovine rotavirus
650		4	\|a BLS
650		4	\|a VP8
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700	0		\|a María José Dus Santos \|e verfasserin \|4 aut
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912			\|a GBV_ILN_70
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912			\|a GBV_ILN_74
912			\|a GBV_ILN_95
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
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912			\|a GBV_ILN_170
912			\|a GBV_ILN_213
912			\|a GBV_ILN_230
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
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912			\|a GBV_ILN_2003
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912			\|a GBV_ILN_4305
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allfields	10.3389/fpls.2015.01170 doi (DE-627)DOAJ015899586 (DE-599)DOAJ1332a89adca8457487e93634f1161602 DE-627 ger DE-627 rakwb eng SB1-1110 Edgardo Federico Alfano verfasserin aut Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Lumazine synthase from Brucella spp. (BLS) is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity.The inner core domain (VP8d) of VP8 spike protein from bovine rotavirus (BRV) is responsible for viral adhesion to sialic acid residues and infection. It also displays neutralizing epitopes, making it a good candidate for vaccination.In this work, the BLS scaffold was assessed for the first time in plants for recombinant vaccine development by N-terminally fusing BLS to VP8d and expressing the resulting fusion (BLSVP8d) in tobacco chloroplasts. Transplastomic plants were obtained and characterized by Southern, northern and western blot. BLSVP8d was highly expressed, representing 40% of total soluble protein (TSP) (4.85 mg/g fresh tissue). BLSVP8d remained soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature. Soluble protein extracts from fresh and lyophilized leaves were able to induce specific neutralizing IgY antibodies in a laying hen model. This work presents BLS as an interesting platform for highly immunogenic injectable, or even oral, subunit vaccines. Lyophilization of transplastomic leaves expressing stable antigenic fusions to BLS would further reduce costs and simplify downstream processing, purification and storage, allowing for more practical vaccines. Tobacco Vaccine IgY Bovine rotavirus BLS VP8 Plant culture Ezequiel Matías Lentz verfasserin aut Demian eBellido verfasserin aut María José Dus Santos verfasserin aut Fernando Alberto Goldbaum verfasserin aut Andrés eWigdorovitz verfasserin aut Fernando Félix Bravo-Almonacid verfasserin aut Fernando Félix Bravo-Almonacid verfasserin aut In Frontiers in Plant Science Frontiers Media S.A., 2011 6(2015) (DE-627)662359240 (DE-600)2613694-6 1664462X nnns volume:6 year:2015 https://doi.org/10.3389/fpls.2015.01170 kostenfrei https://doaj.org/article/1332a89adca8457487e93634f1161602 kostenfrei http://journal.frontiersin.org/Journal/10.3389/fpls.2015.01170/full kostenfrei https://doaj.org/toc/1664-462X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 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 6 2015
spelling	10.3389/fpls.2015.01170 doi (DE-627)DOAJ015899586 (DE-599)DOAJ1332a89adca8457487e93634f1161602 DE-627 ger DE-627 rakwb eng SB1-1110 Edgardo Federico Alfano verfasserin aut Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Lumazine synthase from Brucella spp. (BLS) is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity.The inner core domain (VP8d) of VP8 spike protein from bovine rotavirus (BRV) is responsible for viral adhesion to sialic acid residues and infection. It also displays neutralizing epitopes, making it a good candidate for vaccination.In this work, the BLS scaffold was assessed for the first time in plants for recombinant vaccine development by N-terminally fusing BLS to VP8d and expressing the resulting fusion (BLSVP8d) in tobacco chloroplasts. Transplastomic plants were obtained and characterized by Southern, northern and western blot. BLSVP8d was highly expressed, representing 40% of total soluble protein (TSP) (4.85 mg/g fresh tissue). BLSVP8d remained soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature. Soluble protein extracts from fresh and lyophilized leaves were able to induce specific neutralizing IgY antibodies in a laying hen model. This work presents BLS as an interesting platform for highly immunogenic injectable, or even oral, subunit vaccines. Lyophilization of transplastomic leaves expressing stable antigenic fusions to BLS would further reduce costs and simplify downstream processing, purification and storage, allowing for more practical vaccines. Tobacco Vaccine IgY Bovine rotavirus BLS VP8 Plant culture Ezequiel Matías Lentz verfasserin aut Demian eBellido verfasserin aut María José Dus Santos verfasserin aut Fernando Alberto Goldbaum verfasserin aut Andrés eWigdorovitz verfasserin aut Fernando Félix Bravo-Almonacid verfasserin aut Fernando Félix Bravo-Almonacid verfasserin aut In Frontiers in Plant Science Frontiers Media S.A., 2011 6(2015) (DE-627)662359240 (DE-600)2613694-6 1664462X nnns volume:6 year:2015 https://doi.org/10.3389/fpls.2015.01170 kostenfrei https://doaj.org/article/1332a89adca8457487e93634f1161602 kostenfrei http://journal.frontiersin.org/Journal/10.3389/fpls.2015.01170/full kostenfrei https://doaj.org/toc/1664-462X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 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 6 2015
allfields_unstemmed	10.3389/fpls.2015.01170 doi (DE-627)DOAJ015899586 (DE-599)DOAJ1332a89adca8457487e93634f1161602 DE-627 ger DE-627 rakwb eng SB1-1110 Edgardo Federico Alfano verfasserin aut Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Lumazine synthase from Brucella spp. (BLS) is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity.The inner core domain (VP8d) of VP8 spike protein from bovine rotavirus (BRV) is responsible for viral adhesion to sialic acid residues and infection. It also displays neutralizing epitopes, making it a good candidate for vaccination.In this work, the BLS scaffold was assessed for the first time in plants for recombinant vaccine development by N-terminally fusing BLS to VP8d and expressing the resulting fusion (BLSVP8d) in tobacco chloroplasts. Transplastomic plants were obtained and characterized by Southern, northern and western blot. BLSVP8d was highly expressed, representing 40% of total soluble protein (TSP) (4.85 mg/g fresh tissue). BLSVP8d remained soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature. Soluble protein extracts from fresh and lyophilized leaves were able to induce specific neutralizing IgY antibodies in a laying hen model. This work presents BLS as an interesting platform for highly immunogenic injectable, or even oral, subunit vaccines. Lyophilization of transplastomic leaves expressing stable antigenic fusions to BLS would further reduce costs and simplify downstream processing, purification and storage, allowing for more practical vaccines. Tobacco Vaccine IgY Bovine rotavirus BLS VP8 Plant culture Ezequiel Matías Lentz verfasserin aut Demian eBellido verfasserin aut María José Dus Santos verfasserin aut Fernando Alberto Goldbaum verfasserin aut Andrés eWigdorovitz verfasserin aut Fernando Félix Bravo-Almonacid verfasserin aut Fernando Félix Bravo-Almonacid verfasserin aut In Frontiers in Plant Science Frontiers Media S.A., 2011 6(2015) (DE-627)662359240 (DE-600)2613694-6 1664462X nnns volume:6 year:2015 https://doi.org/10.3389/fpls.2015.01170 kostenfrei https://doaj.org/article/1332a89adca8457487e93634f1161602 kostenfrei http://journal.frontiersin.org/Journal/10.3389/fpls.2015.01170/full kostenfrei https://doaj.org/toc/1664-462X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 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 6 2015
allfieldsGer	10.3389/fpls.2015.01170 doi (DE-627)DOAJ015899586 (DE-599)DOAJ1332a89adca8457487e93634f1161602 DE-627 ger DE-627 rakwb eng SB1-1110 Edgardo Federico Alfano verfasserin aut Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Lumazine synthase from Brucella spp. (BLS) is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity.The inner core domain (VP8d) of VP8 spike protein from bovine rotavirus (BRV) is responsible for viral adhesion to sialic acid residues and infection. It also displays neutralizing epitopes, making it a good candidate for vaccination.In this work, the BLS scaffold was assessed for the first time in plants for recombinant vaccine development by N-terminally fusing BLS to VP8d and expressing the resulting fusion (BLSVP8d) in tobacco chloroplasts. Transplastomic plants were obtained and characterized by Southern, northern and western blot. BLSVP8d was highly expressed, representing 40% of total soluble protein (TSP) (4.85 mg/g fresh tissue). BLSVP8d remained soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature. Soluble protein extracts from fresh and lyophilized leaves were able to induce specific neutralizing IgY antibodies in a laying hen model. This work presents BLS as an interesting platform for highly immunogenic injectable, or even oral, subunit vaccines. Lyophilization of transplastomic leaves expressing stable antigenic fusions to BLS would further reduce costs and simplify downstream processing, purification and storage, allowing for more practical vaccines. Tobacco Vaccine IgY Bovine rotavirus BLS VP8 Plant culture Ezequiel Matías Lentz verfasserin aut Demian eBellido verfasserin aut María José Dus Santos verfasserin aut Fernando Alberto Goldbaum verfasserin aut Andrés eWigdorovitz verfasserin aut Fernando Félix Bravo-Almonacid verfasserin aut Fernando Félix Bravo-Almonacid verfasserin aut In Frontiers in Plant Science Frontiers Media S.A., 2011 6(2015) (DE-627)662359240 (DE-600)2613694-6 1664462X nnns volume:6 year:2015 https://doi.org/10.3389/fpls.2015.01170 kostenfrei https://doaj.org/article/1332a89adca8457487e93634f1161602 kostenfrei http://journal.frontiersin.org/Journal/10.3389/fpls.2015.01170/full kostenfrei https://doaj.org/toc/1664-462X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 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 6 2015
allfieldsSound	10.3389/fpls.2015.01170 doi (DE-627)DOAJ015899586 (DE-599)DOAJ1332a89adca8457487e93634f1161602 DE-627 ger DE-627 rakwb eng SB1-1110 Edgardo Federico Alfano verfasserin aut Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Lumazine synthase from Brucella spp. (BLS) is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity.The inner core domain (VP8d) of VP8 spike protein from bovine rotavirus (BRV) is responsible for viral adhesion to sialic acid residues and infection. It also displays neutralizing epitopes, making it a good candidate for vaccination.In this work, the BLS scaffold was assessed for the first time in plants for recombinant vaccine development by N-terminally fusing BLS to VP8d and expressing the resulting fusion (BLSVP8d) in tobacco chloroplasts. Transplastomic plants were obtained and characterized by Southern, northern and western blot. BLSVP8d was highly expressed, representing 40% of total soluble protein (TSP) (4.85 mg/g fresh tissue). BLSVP8d remained soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature. Soluble protein extracts from fresh and lyophilized leaves were able to induce specific neutralizing IgY antibodies in a laying hen model. This work presents BLS as an interesting platform for highly immunogenic injectable, or even oral, subunit vaccines. Lyophilization of transplastomic leaves expressing stable antigenic fusions to BLS would further reduce costs and simplify downstream processing, purification and storage, allowing for more practical vaccines. Tobacco Vaccine IgY Bovine rotavirus BLS VP8 Plant culture Ezequiel Matías Lentz verfasserin aut Demian eBellido verfasserin aut María José Dus Santos verfasserin aut Fernando Alberto Goldbaum verfasserin aut Andrés eWigdorovitz verfasserin aut Fernando Félix Bravo-Almonacid verfasserin aut Fernando Félix Bravo-Almonacid verfasserin aut In Frontiers in Plant Science Frontiers Media S.A., 2011 6(2015) (DE-627)662359240 (DE-600)2613694-6 1664462X nnns volume:6 year:2015 https://doi.org/10.3389/fpls.2015.01170 kostenfrei https://doaj.org/article/1332a89adca8457487e93634f1161602 kostenfrei http://journal.frontiersin.org/Journal/10.3389/fpls.2015.01170/full kostenfrei https://doaj.org/toc/1664-462X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 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 6 2015
language	English
source	In Frontiers in Plant Science 6(2015) volume:6 year:2015
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topic_facet	Tobacco Vaccine IgY Bovine rotavirus BLS VP8 Plant culture
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container_title	Frontiers in Plant Science
authorswithroles_txt_mv	Edgardo Federico Alfano @@aut@@ Ezequiel Matías Lentz @@aut@@ Demian eBellido @@aut@@ María José Dus Santos @@aut@@ Fernando Alberto Goldbaum @@aut@@ Andrés eWigdorovitz @@aut@@ Fernando Félix Bravo-Almonacid @@aut@@
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callnumber-first	S - Agriculture
author	Edgardo Federico Alfano
spellingShingle	Edgardo Federico Alfano misc SB1-1110 misc Tobacco misc Vaccine misc IgY misc Bovine rotavirus misc BLS misc VP8 misc Plant culture Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts
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topic_title	SB1-1110 Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts Tobacco Vaccine IgY Bovine rotavirus BLS VP8
topic	misc SB1-1110 misc Tobacco misc Vaccine misc IgY misc Bovine rotavirus misc BLS misc VP8 misc Plant culture
topic_unstemmed	misc SB1-1110 misc Tobacco misc Vaccine misc IgY misc Bovine rotavirus misc BLS misc VP8 misc Plant culture
topic_browse	misc SB1-1110 misc Tobacco misc Vaccine misc IgY misc Bovine rotavirus misc BLS misc VP8 misc Plant culture
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title	Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts
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title_full	Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts
author_sort	Edgardo Federico Alfano
journal	Frontiers in Plant Science
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author_browse	Edgardo Federico Alfano Ezequiel Matías Lentz Demian eBellido María José Dus Santos Fernando Alberto Goldbaum Andrés eWigdorovitz Fernando Félix Bravo-Almonacid
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author-letter	Edgardo Federico Alfano
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title_sort	expression of the multimeric and highly immunogenic brucella spp. lumazine synthase fused to bovine rotavirus vp8d as a scaffold for antigen production in tobacco chloroplasts
callnumber	SB1-1110
title_auth	Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts
abstract	Lumazine synthase from Brucella spp. (BLS) is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity.The inner core domain (VP8d) of VP8 spike protein from bovine rotavirus (BRV) is responsible for viral adhesion to sialic acid residues and infection. It also displays neutralizing epitopes, making it a good candidate for vaccination.In this work, the BLS scaffold was assessed for the first time in plants for recombinant vaccine development by N-terminally fusing BLS to VP8d and expressing the resulting fusion (BLSVP8d) in tobacco chloroplasts. Transplastomic plants were obtained and characterized by Southern, northern and western blot. BLSVP8d was highly expressed, representing 40% of total soluble protein (TSP) (4.85 mg/g fresh tissue). BLSVP8d remained soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature. Soluble protein extracts from fresh and lyophilized leaves were able to induce specific neutralizing IgY antibodies in a laying hen model. This work presents BLS as an interesting platform for highly immunogenic injectable, or even oral, subunit vaccines. Lyophilization of transplastomic leaves expressing stable antigenic fusions to BLS would further reduce costs and simplify downstream processing, purification and storage, allowing for more practical vaccines.
abstractGer	Lumazine synthase from Brucella spp. (BLS) is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity.The inner core domain (VP8d) of VP8 spike protein from bovine rotavirus (BRV) is responsible for viral adhesion to sialic acid residues and infection. It also displays neutralizing epitopes, making it a good candidate for vaccination.In this work, the BLS scaffold was assessed for the first time in plants for recombinant vaccine development by N-terminally fusing BLS to VP8d and expressing the resulting fusion (BLSVP8d) in tobacco chloroplasts. Transplastomic plants were obtained and characterized by Southern, northern and western blot. BLSVP8d was highly expressed, representing 40% of total soluble protein (TSP) (4.85 mg/g fresh tissue). BLSVP8d remained soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature. Soluble protein extracts from fresh and lyophilized leaves were able to induce specific neutralizing IgY antibodies in a laying hen model. This work presents BLS as an interesting platform for highly immunogenic injectable, or even oral, subunit vaccines. Lyophilization of transplastomic leaves expressing stable antigenic fusions to BLS would further reduce costs and simplify downstream processing, purification and storage, allowing for more practical vaccines.
abstract_unstemmed	Lumazine synthase from Brucella spp. (BLS) is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity.The inner core domain (VP8d) of VP8 spike protein from bovine rotavirus (BRV) is responsible for viral adhesion to sialic acid residues and infection. It also displays neutralizing epitopes, making it a good candidate for vaccination.In this work, the BLS scaffold was assessed for the first time in plants for recombinant vaccine development by N-terminally fusing BLS to VP8d and expressing the resulting fusion (BLSVP8d) in tobacco chloroplasts. Transplastomic plants were obtained and characterized by Southern, northern and western blot. BLSVP8d was highly expressed, representing 40% of total soluble protein (TSP) (4.85 mg/g fresh tissue). BLSVP8d remained soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature. Soluble protein extracts from fresh and lyophilized leaves were able to induce specific neutralizing IgY antibodies in a laying hen model. This work presents BLS as an interesting platform for highly immunogenic injectable, or even oral, subunit vaccines. Lyophilization of transplastomic leaves expressing stable antigenic fusions to BLS would further reduce costs and simplify downstream processing, purification and storage, allowing for more practical vaccines.
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title_short	Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts
url	https://doi.org/10.3389/fpls.2015.01170 https://doaj.org/article/1332a89adca8457487e93634f1161602 http://journal.frontiersin.org/Journal/10.3389/fpls.2015.01170/full https://doaj.org/toc/1664-462X
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author2	Ezequiel Matías Lentz Demian eBellido María José Dus Santos Fernando Alberto Goldbaum Andrés eWigdorovitz Fernando Félix Bravo-Almonacid
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up_date	2024-07-03T17:46:16.654Z
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It also displays neutralizing epitopes, making it a good candidate for vaccination.In this work, the BLS scaffold was assessed for the first time in plants for recombinant vaccine development by N-terminally fusing BLS to VP8d and expressing the resulting fusion (BLSVP8d) in tobacco chloroplasts. Transplastomic plants were obtained and characterized by Southern, northern and western blot. BLSVP8d was highly expressed, representing 40% of total soluble protein (TSP) (4.85 mg/g fresh tissue). BLSVP8d remained soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature. Soluble protein extracts from fresh and lyophilized leaves were able to induce specific neutralizing IgY antibodies in a laying hen model. This work presents BLS as an interesting platform for highly immunogenic injectable, or even oral, subunit vaccines. 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Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8d as a scaffold for antigen production in tobacco chloroplasts

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