Functional characterization of a plant-produced infectious bursal disease virus antigen fused to the constant region of avian IgY immunoglobulins
Infectious bursal disease virus (IBDV) is the cause of an economically important highly contagious disease of poultry, and vaccines are regarded as the most beneficial interventions for its prevention. In this study, plants were used to produce a recombinant chimeric IBDV antigen for the formulation...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2019-09, Vol.103 (18), p.7491-7504 |
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| creator | Rage, Emile Drissi Touzani, Charifa Marusic, Carla Lico, Chiara Göbel, Thomas Bortolami, Alessio Bonfante, Francesco Salzano, Anna Maria Scaloni, Andrea Fellahi, Siham El Houadfi, Mohammed Donini, Marcello Baschieri, Selene |
| description | Infectious bursal disease virus (IBDV) is the cause of an economically important highly contagious disease of poultry, and vaccines are regarded as the most beneficial interventions for its prevention. In this study, plants were used to produce a recombinant chimeric IBDV antigen for the formulation of an innovative subunit vaccine. The fusion protein (PD-FcY) was designed to combine the immunodominant projection domain (PD) of the viral structural protein VP2 with the constant region of avian IgY (FcY), which was selected to enhance antigen uptake by avian immune cells. The gene construct encoding the fusion protein was transiently expressed in
Nicotiana benthamiana
plants and an extraction/purification protocol was set up, allowing to reduce the contamination by undesired plant compounds/proteins. Mass spectrometry analysis of the purified protein revealed that the glycosylation pattern of the FcY portion was similar to that observed in native IgY, while in vitro assays demonstrated the ability of PD-FcY to bind to the avian immunoglobulin receptor CHIR-AB1. Preliminary immunization studies proved that PD-FcY was able to induce the production of protective anti-IBDV-VP2 antibodies in chickens. In conclusion, the proposed fusion strategy holds promises for the development of innovative low-cost subunit vaccines for the prevention of avian viral diseases. |
| doi_str_mv | 10.1007/s00253-019-09992-9 |
| format | Article |
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Nicotiana benthamiana
plants and an extraction/purification protocol was set up, allowing to reduce the contamination by undesired plant compounds/proteins. Mass spectrometry analysis of the purified protein revealed that the glycosylation pattern of the FcY portion was similar to that observed in native IgY, while in vitro assays demonstrated the ability of PD-FcY to bind to the avian immunoglobulin receptor CHIR-AB1. Preliminary immunization studies proved that PD-FcY was able to induce the production of protective anti-IBDV-VP2 antibodies in chickens. In conclusion, the proposed fusion strategy holds promises for the development of innovative low-cost subunit vaccines for the prevention of avian viral diseases.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-019-09992-9</identifier><identifier>PMID: 31332484</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Analysis ; Animals ; Antibodies ; Antibodies, Viral - blood ; Antigens ; Antigens, Viral - biosynthesis ; Antigens, Viral - immunology ; B cells ; Biomedical and Life Sciences ; Biotechnological Products and Process Engineering ; Biotechnology ; Chickens ; Chickens - immunology ; Constant region ; Contamination ; Disease ; Economic importance ; Fusion protein ; Glycosylation ; Immune system ; Immunization ; Immunoglobulins ; Immunoglobulins - biosynthesis ; Immunoglobulins - immunology ; Infectious bursal disease ; Infectious bursal disease virus ; Life Sciences ; Mass spectrometry ; Mass spectroscopy ; Microbial Genetics and Genomics ; Microbiology ; Nicotiana - genetics ; Plant diseases ; Plant extracts ; Plant viruses ; Poultry Diseases - prevention & control ; Poultry Diseases - virology ; Prevention ; Protein purification ; Proteins ; Scientific equipment and supplies industry ; Vaccination ; Vaccines ; Vaccines, Subunit - biosynthesis ; Viral antibodies ; Viral diseases ; Viral Structural Proteins - biosynthesis ; Viral Structural Proteins - immunology ; Viral Vaccines - biosynthesis ; Viruses</subject><ispartof>Applied microbiology and biotechnology, 2019-09, Vol.103 (18), p.7491-7504</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2019</rights><rights>COPYRIGHT 2019 Springer</rights><rights>Applied Microbiology and Biotechnology is a copyright of Springer, (2019). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-55a73455d9bb41d29e31d103e676d9df2c0918172601e6ec6a022f77d7c919663</citedby><cites>FETCH-LOGICAL-c557t-55a73455d9bb41d29e31d103e676d9df2c0918172601e6ec6a022f77d7c919663</cites><orcidid>0000-0001-9183-0728</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-019-09992-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-019-09992-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31332484$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rage, Emile</creatorcontrib><creatorcontrib>Drissi Touzani, Charifa</creatorcontrib><creatorcontrib>Marusic, Carla</creatorcontrib><creatorcontrib>Lico, Chiara</creatorcontrib><creatorcontrib>Göbel, Thomas</creatorcontrib><creatorcontrib>Bortolami, Alessio</creatorcontrib><creatorcontrib>Bonfante, Francesco</creatorcontrib><creatorcontrib>Salzano, Anna Maria</creatorcontrib><creatorcontrib>Scaloni, Andrea</creatorcontrib><creatorcontrib>Fellahi, Siham</creatorcontrib><creatorcontrib>El Houadfi, Mohammed</creatorcontrib><creatorcontrib>Donini, Marcello</creatorcontrib><creatorcontrib>Baschieri, Selene</creatorcontrib><title>Functional characterization of a plant-produced infectious bursal disease virus antigen fused to the constant region of avian IgY immunoglobulins</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Infectious bursal disease virus (IBDV) is the cause of an economically important highly contagious disease of poultry, and vaccines are regarded as the most beneficial interventions for its prevention. In this study, plants were used to produce a recombinant chimeric IBDV antigen for the formulation of an innovative subunit vaccine. The fusion protein (PD-FcY) was designed to combine the immunodominant projection domain (PD) of the viral structural protein VP2 with the constant region of avian IgY (FcY), which was selected to enhance antigen uptake by avian immune cells. The gene construct encoding the fusion protein was transiently expressed in
Nicotiana benthamiana
plants and an extraction/purification protocol was set up, allowing to reduce the contamination by undesired plant compounds/proteins. Mass spectrometry analysis of the purified protein revealed that the glycosylation pattern of the FcY portion was similar to that observed in native IgY, while in vitro assays demonstrated the ability of PD-FcY to bind to the avian immunoglobulin receptor CHIR-AB1. Preliminary immunization studies proved that PD-FcY was able to induce the production of protective anti-IBDV-VP2 antibodies in chickens. In conclusion, the proposed fusion strategy holds promises for the development of innovative low-cost subunit vaccines for the prevention of avian viral diseases.</description><subject>Analysis</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Viral - blood</subject><subject>Antigens</subject><subject>Antigens, Viral - biosynthesis</subject><subject>Antigens, Viral - immunology</subject><subject>B cells</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnological Products and Process Engineering</subject><subject>Biotechnology</subject><subject>Chickens</subject><subject>Chickens - immunology</subject><subject>Constant region</subject><subject>Contamination</subject><subject>Disease</subject><subject>Economic importance</subject><subject>Fusion protein</subject><subject>Glycosylation</subject><subject>Immune system</subject><subject>Immunization</subject><subject>Immunoglobulins</subject><subject>Immunoglobulins - biosynthesis</subject><subject>Immunoglobulins - immunology</subject><subject>Infectious bursal disease</subject><subject>Infectious bursal disease virus</subject><subject>Life Sciences</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Nicotiana - genetics</subject><subject>Plant diseases</subject><subject>Plant extracts</subject><subject>Plant viruses</subject><subject>Poultry Diseases - prevention & control</subject><subject>Poultry Diseases - virology</subject><subject>Prevention</subject><subject>Protein purification</subject><subject>Proteins</subject><subject>Scientific equipment and supplies industry</subject><subject>Vaccination</subject><subject>Vaccines</subject><subject>Vaccines, Subunit - biosynthesis</subject><subject>Viral antibodies</subject><subject>Viral diseases</subject><subject>Viral Structural Proteins - biosynthesis</subject><subject>Viral Structural Proteins - immunology</subject><subject>Viral Vaccines - 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Academic</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rage, Emile</au><au>Drissi Touzani, Charifa</au><au>Marusic, Carla</au><au>Lico, Chiara</au><au>Göbel, Thomas</au><au>Bortolami, Alessio</au><au>Bonfante, Francesco</au><au>Salzano, Anna Maria</au><au>Scaloni, Andrea</au><au>Fellahi, Siham</au><au>El Houadfi, Mohammed</au><au>Donini, Marcello</au><au>Baschieri, Selene</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional characterization of a plant-produced infectious bursal disease virus antigen fused to the constant region of avian IgY immunoglobulins</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2019-09-01</date><risdate>2019</risdate><volume>103</volume><issue>18</issue><spage>7491</spage><epage>7504</epage><pages>7491-7504</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>Infectious bursal disease virus (IBDV) is the cause of an economically important highly contagious disease of poultry, and vaccines are regarded as the most beneficial interventions for its prevention. In this study, plants were used to produce a recombinant chimeric IBDV antigen for the formulation of an innovative subunit vaccine. The fusion protein (PD-FcY) was designed to combine the immunodominant projection domain (PD) of the viral structural protein VP2 with the constant region of avian IgY (FcY), which was selected to enhance antigen uptake by avian immune cells. The gene construct encoding the fusion protein was transiently expressed in
Nicotiana benthamiana
plants and an extraction/purification protocol was set up, allowing to reduce the contamination by undesired plant compounds/proteins. Mass spectrometry analysis of the purified protein revealed that the glycosylation pattern of the FcY portion was similar to that observed in native IgY, while in vitro assays demonstrated the ability of PD-FcY to bind to the avian immunoglobulin receptor CHIR-AB1. Preliminary immunization studies proved that PD-FcY was able to induce the production of protective anti-IBDV-VP2 antibodies in chickens. In conclusion, the proposed fusion strategy holds promises for the development of innovative low-cost subunit vaccines for the prevention of avian viral diseases.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>31332484</pmid><doi>10.1007/s00253-019-09992-9</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0001-9183-0728</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 2019-09, Vol.103 (18), p.7491-7504 |
| issn | 0175-7598 1432-0614 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2283107111 |
| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Analysis Animals Antibodies Antibodies, Viral - blood Antigens Antigens, Viral - biosynthesis Antigens, Viral - immunology B cells Biomedical and Life Sciences Biotechnological Products and Process Engineering Biotechnology Chickens Chickens - immunology Constant region Contamination Disease Economic importance Fusion protein Glycosylation Immune system Immunization Immunoglobulins Immunoglobulins - biosynthesis Immunoglobulins - immunology Infectious bursal disease Infectious bursal disease virus Life Sciences Mass spectrometry Mass spectroscopy Microbial Genetics and Genomics Microbiology Nicotiana - genetics Plant diseases Plant extracts Plant viruses Poultry Diseases - prevention & control Poultry Diseases - virology Prevention Protein purification Proteins Scientific equipment and supplies industry Vaccination Vaccines Vaccines, Subunit - biosynthesis Viral antibodies Viral diseases Viral Structural Proteins - biosynthesis Viral Structural Proteins - immunology Viral Vaccines - biosynthesis Viruses |
| title | Functional characterization of a plant-produced infectious bursal disease virus antigen fused to the constant region of avian IgY immunoglobulins |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T13%3A46%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Functional%20characterization%20of%20a%20plant-produced%20infectious%20bursal%20disease%20virus%20antigen%20fused%20to%20the%20constant%20region%20of%20avian%20IgY%20immunoglobulins&rft.jtitle=Applied%20microbiology%20and%20biotechnology&rft.au=Rage,%20Emile&rft.date=2019-09-01&rft.volume=103&rft.issue=18&rft.spage=7491&rft.epage=7504&rft.pages=7491-7504&rft.issn=0175-7598&rft.eissn=1432-0614&rft_id=info:doi/10.1007/s00253-019-09992-9&rft_dat=%3Cgale_proqu%3EA597980575%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2261986864&rft_id=info:pmid/31332484&rft_galeid=A597980575&rfr_iscdi=true |