Epitope Presentation of Dengue Viral Envelope Glycoprotein Domain III on Hepatitis B Core Protein Virus-Like Particles Produced in Nicotiana benthamiana.
Identifieur interne : 000120 ( Main/Exploration ); précédent : 000119; suivant : 000121Epitope Presentation of Dengue Viral Envelope Glycoprotein Domain III on Hepatitis B Core Protein Virus-Like Particles Produced in Nicotiana benthamiana.
Auteurs : Ee Leen Pang [Malaisie] ; Hadrien Peyret [Royaume-Uni] ; Alex Ramirez [Royaume-Uni] ; Hwei-San Loh [Malaisie] ; Kok-Song Lai [Malaisie] ; Chee-Mun Fang [Malaisie] ; William M. Rosenberg [Royaume-Uni] ; George P. Lomonossoff [Royaume-Uni]Source :
- Frontiers in plant science [ 1664-462X ] ; 2019.
Abstract
Dengue fever is currently ranked as the top emerging tropical disease, driven by increased global travel, urbanization, and poor hygiene conditions as well as global warming effects which facilitate the spread of Aedes mosquitoes beyond their current distribution. Today, more than 100 countries are affected most of which are tropical Asian and Latin American nations with limited access to medical care. Hence, the development of a dengue vaccine that is dually cost-effective and able to confer a comprehensive protection is ultimately needed. In this study, a consensus sequence of the antigenic dengue viral glycoprotein domain III (cEDIII) was used aiming to provide comprehensive coverage against all four circulating dengue viral serotypes and potential clade replacement event. Utilizing hepatitis B tandem core technology, the cEDIII sequence was inserted into the immunodominant c/e1 loop region so that it could be displayed on the spike structures of assembled particles. The tandem core particles displaying cEDIII epitopes (tHBcAg-cEDIII) were successfully produced in Nicotiana benthamiana via Agrobacterium-mediated transient expression strategy to give a protein of ∼54 kDa, detected in both soluble and insoluble fractions of plant extracts. The assembled tHBcAg-cEDIII virus-like particles (VLPs) were also visualized from transmission electron microscopy. These VLPs had diameters that range from 32 to 35 nm, presenting an apparent size increment as compared to tHBcAg control particles without cEDIII display (namely tEL). Mice immunized with tHBcAg-cEDIII VLPs showed a positive seroconversion to cEDIII antigen, thereby signifying that the assembled tHBcAg-cEDIII VLPs have successfully displayed cEDIII antigen to the immune system. If it is proven to be successful, tHBcAg-cEDIII has the potential to be developed as a cost-effective vaccine candidate that confers a simultaneous protection against all four infecting dengue viral serotypes.
DOI: 10.3389/fpls.2019.00455
PubMed: 31057572
PubMed Central: PMC6477658
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Epitope Presentation of Dengue Viral Envelope Glycoprotein Domain III on Hepatitis B Core Protein Virus-Like Particles Produced in <i>Nicotiana benthamiana</i>.</title><author><name sortKey="Pang, Ee Leen" sort="Pang, Ee Leen" uniqKey="Pang E" first="Ee Leen" last="Pang">Ee Leen Pang</name><affiliation wicri:level="1"><nlm:affiliation>School of Biosciences, University of Nottingham Malaysia, Semenyih, Malaysia.</nlm:affiliation><country xml:lang="fr">Malaisie</country><wicri:regionArea>School of Biosciences, University of Nottingham Malaysia, Semenyih</wicri:regionArea><wicri:noRegion>Semenyih</wicri:noRegion></affiliation></author><author><name sortKey="Peyret, Hadrien" sort="Peyret, Hadrien" uniqKey="Peyret H" first="Hadrien" last="Peyret">Hadrien Peyret</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Biological Chemistry, John Innes Centre, Norwich</wicri:regionArea><wicri:noRegion>Norwich</wicri:noRegion></affiliation></author><author><name sortKey="Ramirez, Alex" sort="Ramirez, Alex" uniqKey="Ramirez A" first="Alex" last="Ramirez">Alex Ramirez</name><affiliation wicri:level="3"><nlm:affiliation>iQur Limited, London, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>iQur Limited, London</wicri:regionArea><placeName><settlement type="city">Londres</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Grand Londres</region></placeName></affiliation></author><author><name sortKey="Loh, Hwei San" sort="Loh, Hwei San" uniqKey="Loh H" first="Hwei-San" last="Loh">Hwei-San Loh</name><affiliation wicri:level="1"><nlm:affiliation>School of Biosciences, University of Nottingham Malaysia, Semenyih, Malaysia.</nlm:affiliation><country xml:lang="fr">Malaisie</country><wicri:regionArea>School of Biosciences, University of Nottingham Malaysia, Semenyih</wicri:regionArea><wicri:noRegion>Semenyih</wicri:noRegion></affiliation></author><author><name sortKey="Lai, Kok Song" sort="Lai, Kok Song" uniqKey="Lai K" first="Kok-Song" last="Lai">Kok-Song Lai</name><affiliation wicri:level="1"><nlm:affiliation>Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Malaysia.</nlm:affiliation><country xml:lang="fr">Malaisie</country><wicri:regionArea>Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang</wicri:regionArea><wicri:noRegion>Serdang</wicri:noRegion></affiliation></author><author><name sortKey="Fang, Chee Mun" sort="Fang, Chee Mun" uniqKey="Fang C" first="Chee-Mun" last="Fang">Chee-Mun Fang</name><affiliation wicri:level="1"><nlm:affiliation>Division of Biomedical Sciences, School of Pharmacy, University of Nottingham Malaysia, Semenyih, Malaysia.</nlm:affiliation><country xml:lang="fr">Malaisie</country><wicri:regionArea>Division of Biomedical Sciences, School of Pharmacy, University of Nottingham Malaysia, Semenyih</wicri:regionArea><wicri:noRegion>Semenyih</wicri:noRegion></affiliation></author><author><name sortKey="Rosenberg, William M" sort="Rosenberg, William M" uniqKey="Rosenberg W" first="William M" last="Rosenberg">William M. 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Rosenberg</name><affiliation wicri:level="3"><nlm:affiliation>iQur Limited, London, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>iQur Limited, London</wicri:regionArea><placeName><settlement type="city">Londres</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Grand Londres</region></placeName></affiliation></author><author><name sortKey="Lomonossoff, George P" sort="Lomonossoff, George P" uniqKey="Lomonossoff G" first="George P" last="Lomonossoff">George P. Lomonossoff</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Biological Chemistry, John Innes Centre, Norwich</wicri:regionArea><wicri:noRegion>Norwich</wicri:noRegion></affiliation></author></analytic><series><title level="j">Frontiers in plant science</title><idno type="ISSN">1664-462X</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Dengue fever is currently ranked as the top emerging tropical disease, driven by increased global travel, urbanization, and poor hygiene conditions as well as global warming effects which facilitate the spread of <i>Aedes</i> mosquitoes beyond their current distribution. Today, more than 100 countries are affected most of which are tropical Asian and Latin American nations with limited access to medical care. Hence, the development of a dengue vaccine that is dually cost-effective and able to confer a comprehensive protection is ultimately needed. In this study, a consensus sequence of the antigenic dengue viral glycoprotein domain III (cEDIII) was used aiming to provide comprehensive coverage against all four circulating dengue viral serotypes and potential clade replacement event. Utilizing hepatitis B tandem core technology, the cEDIII sequence was inserted into the immunodominant c/e1 loop region so that it could be displayed on the spike structures of assembled particles. The tandem core particles displaying cEDIII epitopes (tHBcAg-cEDIII) were successfully produced in <i>Nicotiana benthamiana</i> via <i>Agrobacterium</i>-mediated transient expression strategy to give a protein of ∼54 kDa, detected in both soluble and insoluble fractions of plant extracts. The assembled tHBcAg-cEDIII virus-like particles (VLPs) were also visualized from transmission electron microscopy. These VLPs had diameters that range from 32 to 35 nm, presenting an apparent size increment as compared to tHBcAg control particles without cEDIII display (namely tEL). Mice immunized with tHBcAg-cEDIII VLPs showed a positive seroconversion to cEDIII antigen, thereby signifying that the assembled tHBcAg-cEDIII VLPs have successfully displayed cEDIII antigen to the immune system. If it is proven to be successful, tHBcAg-cEDIII has the potential to be developed as a cost-effective vaccine candidate that confers a simultaneous protection against all four infecting dengue viral serotypes.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">31057572</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>28</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1664-462X</ISSN><JournalIssue CitedMedium="Print"><Volume>10</Volume><PubDate><Year>2019</Year></PubDate></JournalIssue><Title>Frontiers in plant science</Title><ISOAbbreviation>Front Plant Sci</ISOAbbreviation></Journal><ArticleTitle>Epitope Presentation of Dengue Viral Envelope Glycoprotein Domain III on Hepatitis B Core Protein Virus-Like Particles Produced in <i>Nicotiana benthamiana</i>.</ArticleTitle><Pagination><MedlinePgn>455</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fpls.2019.00455</ELocationID><Abstract><AbstractText>Dengue fever is currently ranked as the top emerging tropical disease, driven by increased global travel, urbanization, and poor hygiene conditions as well as global warming effects which facilitate the spread of <i>Aedes</i> mosquitoes beyond their current distribution. Today, more than 100 countries are affected most of which are tropical Asian and Latin American nations with limited access to medical care. Hence, the development of a dengue vaccine that is dually cost-effective and able to confer a comprehensive protection is ultimately needed. In this study, a consensus sequence of the antigenic dengue viral glycoprotein domain III (cEDIII) was used aiming to provide comprehensive coverage against all four circulating dengue viral serotypes and potential clade replacement event. Utilizing hepatitis B tandem core technology, the cEDIII sequence was inserted into the immunodominant c/e1 loop region so that it could be displayed on the spike structures of assembled particles. The tandem core particles displaying cEDIII epitopes (tHBcAg-cEDIII) were successfully produced in <i>Nicotiana benthamiana</i> via <i>Agrobacterium</i>-mediated transient expression strategy to give a protein of ∼54 kDa, detected in both soluble and insoluble fractions of plant extracts. The assembled tHBcAg-cEDIII virus-like particles (VLPs) were also visualized from transmission electron microscopy. These VLPs had diameters that range from 32 to 35 nm, presenting an apparent size increment as compared to tHBcAg control particles without cEDIII display (namely tEL). Mice immunized with tHBcAg-cEDIII VLPs showed a positive seroconversion to cEDIII antigen, thereby signifying that the assembled tHBcAg-cEDIII VLPs have successfully displayed cEDIII antigen to the immune system. If it is proven to be successful, tHBcAg-cEDIII has the potential to be developed as a cost-effective vaccine candidate that confers a simultaneous protection against all four infecting dengue viral serotypes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pang</LastName><ForeName>Ee Leen</ForeName><Initials>EL</Initials><AffiliationInfo><Affiliation>School of Biosciences, University of Nottingham Malaysia, Semenyih, Malaysia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peyret</LastName><ForeName>Hadrien</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ramirez</LastName><ForeName>Alex</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>iQur Limited, London, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Loh</LastName><ForeName>Hwei-San</ForeName><Initials>HS</Initials><AffiliationInfo><Affiliation>School of Biosciences, University of Nottingham Malaysia, Semenyih, Malaysia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lai</LastName><ForeName>Kok-Song</ForeName><Initials>KS</Initials><AffiliationInfo><Affiliation>Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Malaysia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fang</LastName><ForeName>Chee-Mun</ForeName><Initials>CM</Initials><AffiliationInfo><Affiliation>Division of Biomedical Sciences, School of Pharmacy, University of Nottingham Malaysia, Semenyih, Malaysia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rosenberg</LastName><ForeName>William M</ForeName><Initials>WM</Initials><AffiliationInfo><Affiliation>iQur Limited, London, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lomonossoff</LastName><ForeName>George P</ForeName><Initials>GP</Initials><AffiliationInfo><Affiliation>Department of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>BBS/E/J/00000166</GrantID><Acronym>BB_</Acronym><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>BBS/E/J/0000A182</GrantID><Acronym>BB_</Acronym><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>04</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Front Plant Sci</MedlineTA><NlmUniqueID>101568200</NlmUniqueID><ISSNLinking>1664-462X</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">dengue envelope glycoprotein</Keyword><Keyword MajorTopicYN="N">dengue vaccine</Keyword><Keyword MajorTopicYN="N">envelope glycoprotein domain III</Keyword><Keyword MajorTopicYN="N">epitope display</Keyword><Keyword MajorTopicYN="N">hepatitis B core antigen</Keyword><Keyword MajorTopicYN="N">tandem core technology</Keyword><Keyword MajorTopicYN="N">virus-like particles</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>12</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>03</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>5</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>5</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>5</Month><Day>7</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31057572</ArticleId><ArticleId IdType="doi">10.3389/fpls.2019.00455</ArticleId><ArticleId IdType="pmc">PMC6477658</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):1915-20</Citation><ArticleIdList><ArticleId IdType="pubmed">10051569</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2000 Oct 25;276(2):364-75</Citation><ArticleIdList><ArticleId IdType="pubmed">11040127</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2001 Aug;75(16):7769-73</Citation><ArticleIdList><ArticleId 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name="Royaume-Uni"><noRegion><name sortKey="Peyret, Hadrien" sort="Peyret, Hadrien" uniqKey="Peyret H" first="Hadrien" last="Peyret">Hadrien Peyret</name></noRegion><name sortKey="Lomonossoff, George P" sort="Lomonossoff, George P" uniqKey="Lomonossoff G" first="George P" last="Lomonossoff">George P. Lomonossoff</name><name sortKey="Ramirez, Alex" sort="Ramirez, Alex" uniqKey="Ramirez A" first="Alex" last="Ramirez">Alex Ramirez</name><name sortKey="Rosenberg, William M" sort="Rosenberg, William M" uniqKey="Rosenberg W" first="William M" last="Rosenberg">William M. Rosenberg</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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