Expression and purification of an influenza hemagglutinin—one step closer to a recombinant protein-based influenza vaccine
Identifieur interne : 000E29 ( Pmc/Curation ); précédent : 000E28; suivant : 000E30Expression and purification of an influenza hemagglutinin—one step closer to a recombinant protein-based influenza vaccine
Auteurs : Keyang Wang ; Kathleen M. Holtz ; Karl Anderson ; Richard Chubet ; Wafaa Mahmoud ; Manon M. J. CoxSource :
- Vaccine [ 0264-410X ] ; 2005.
Abstract
Numerous human infections with avian influenza viruses in Asia in recent years have raised the concern that the next influenza pandemic is imminent. The most effective way to combat influenza is through the vaccination of the public. However, a minimum of 3–6 months is needed to develop an influenza vaccine using the traditional egg-based vaccine approach. The influenza hemagglutinin protein (HA), the active ingredient in the current vaccine, can be expressed in insect cells using the baculovirus expression vector system and purified rapidly. An influenza vaccine based on such a recombinant antigen allows a more timely response to a potential influenza pandemic. Here, we report an innovative monitoring assay for recombinant HA (rHA) expression and a rapid purification process. Various biochemical analyses indicate that the purified rHA is properly folded and biologically active.
Url:
DOI: 10.1016/j.vaccine.2005.11.005
PubMed: 16310896
PubMed Central: 7115642
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Expression and purification of an influenza hemagglutinin—one step closer to a recombinant protein-based influenza vaccine</title><author><name sortKey="Wang, Keyang" sort="Wang, Keyang" uniqKey="Wang K" first="Keyang" last="Wang">Keyang Wang</name></author><author><name sortKey="Holtz, Kathleen M" sort="Holtz, Kathleen M" uniqKey="Holtz K" first="Kathleen M." last="Holtz">Kathleen M. Holtz</name></author><author><name sortKey="Anderson, Karl" sort="Anderson, Karl" uniqKey="Anderson K" first="Karl" last="Anderson">Karl Anderson</name></author><author><name sortKey="Chubet, Richard" sort="Chubet, Richard" uniqKey="Chubet R" first="Richard" last="Chubet">Richard Chubet</name></author><author><name sortKey="Mahmoud, Wafaa" sort="Mahmoud, Wafaa" uniqKey="Mahmoud W" first="Wafaa" last="Mahmoud">Wafaa Mahmoud</name></author><author><name sortKey="Cox, Manon M J" sort="Cox, Manon M J" uniqKey="Cox M" first="Manon M. J." last="Cox">Manon M. J. Cox</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16310896</idno><idno type="pmc">7115642</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7115642</idno><idno type="RBID">PMC:7115642</idno><idno type="doi">10.1016/j.vaccine.2005.11.005</idno><date when="2005">2005</date><idno type="wicri:Area/Pmc/Corpus">000E29</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000E29</idno><idno type="wicri:Area/Pmc/Curation">000E29</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000E29</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Expression and purification of an influenza hemagglutinin—one step closer to a recombinant protein-based influenza vaccine</title><author><name sortKey="Wang, Keyang" sort="Wang, Keyang" uniqKey="Wang K" first="Keyang" last="Wang">Keyang Wang</name></author><author><name sortKey="Holtz, Kathleen M" sort="Holtz, Kathleen M" uniqKey="Holtz K" first="Kathleen M." last="Holtz">Kathleen M. Holtz</name></author><author><name sortKey="Anderson, Karl" sort="Anderson, Karl" uniqKey="Anderson K" first="Karl" last="Anderson">Karl Anderson</name></author><author><name sortKey="Chubet, Richard" sort="Chubet, Richard" uniqKey="Chubet R" first="Richard" last="Chubet">Richard Chubet</name></author><author><name sortKey="Mahmoud, Wafaa" sort="Mahmoud, Wafaa" uniqKey="Mahmoud W" first="Wafaa" last="Mahmoud">Wafaa Mahmoud</name></author><author><name sortKey="Cox, Manon M J" sort="Cox, Manon M J" uniqKey="Cox M" first="Manon M. J." last="Cox">Manon M. J. Cox</name></author></analytic><series><title level="j">Vaccine</title><idno type="ISSN">0264-410X</idno><idno type="eISSN">1873-2518</idno><imprint><date when="2005">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Numerous human infections with avian influenza viruses in Asia in recent years have raised the concern that the next influenza pandemic is imminent. The most effective way to combat influenza is through the vaccination of the public. However, a minimum of 3–6 months is needed to develop an influenza vaccine using the traditional egg-based vaccine approach. The influenza hemagglutinin protein (HA), the active ingredient in the current vaccine, can be expressed in insect cells using the baculovirus expression vector system and purified rapidly. An influenza vaccine based on such a recombinant antigen allows a more timely response to a potential influenza pandemic. Here, we report an innovative monitoring assay for recombinant HA (rHA) expression and a rapid purification process. Various biochemical analyses indicate that the purified rHA is properly folded and biologically active.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Hilleman, M R" uniqKey="Hilleman M">M.R. Hilleman</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Glezen, W P" uniqKey="Glezen W">W.P. Glezen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cox, N J" uniqKey="Cox N">N.J. Cox</name></author><author><name sortKey="Subbarao, K" uniqKey="Subbarao K">K. Subbarao</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Clements, M L" uniqKey="Clements M">M.L. 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Wilkinson</name></author><author><name sortKey="Vosnesensky, A" uniqKey="Vosnesensky A">A. Vosnesensky</name></author><author><name sortKey="Smith, G" uniqKey="Smith G">G. Smith</name></author><author><name sortKey="Garcia, M" uniqKey="Garcia M">M. Garcia</name></author><author><name sortKey="Stone, H" uniqKey="Stone H">H. Stone</name></author></analytic></biblStruct></listBibl></div1></back></TEI><pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Vaccine</journal-id><journal-id journal-id-type="iso-abbrev">Vaccine</journal-id><journal-title-group><journal-title>Vaccine</journal-title></journal-title-group><issn pub-type="ppub">0264-410X</issn><issn pub-type="epub">1873-2518</issn><publisher><publisher-name>Elsevier Ltd.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">16310896</article-id><article-id pub-id-type="pmc">7115642</article-id><article-id pub-id-type="publisher-id">S0264-410X(05)01130-8</article-id><article-id pub-id-type="doi">10.1016/j.vaccine.2005.11.005</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Expression and purification of an influenza hemagglutinin—one step closer to a recombinant protein-based influenza vaccine</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Wang</surname><given-names>Keyang</given-names></name><email>kwang@proteinsciences.com</email><xref rid="cor1" ref-type="corresp">⁎</xref></contrib><contrib contrib-type="author"><name><surname>Holtz</surname><given-names>Kathleen M.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Anderson</surname><given-names>Karl</given-names></name></contrib><contrib contrib-type="author"><name><surname>Chubet</surname><given-names>Richard</given-names></name></contrib><contrib contrib-type="author"><name><surname>Mahmoud</surname><given-names>Wafaa</given-names></name></contrib><contrib contrib-type="author"><name><surname>Cox</surname><given-names>Manon M.J.</given-names></name></contrib></contrib-group><aff>Protein Sciences Corporation, 1000 Research Parkway, Meriden, CT 06450, USA</aff><author-notes><corresp id="cor1"><label>⁎</label>Corresponding author. Tel.: +1 203 686 0800x328; fax: +1 203 686 0268. <email>kwang@proteinsciences.com</email></corresp></author-notes><pub-date pub-type="pmc-release"><day>10</day><month>11</month><year>2005</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><day>15</day><month>3</month><year>2006</year></pub-date><pub-date pub-type="epub"><day>10</day><month>11</month><year>2005</year></pub-date><volume>24</volume><issue>12</issue><fpage>2176</fpage><lpage>2185</lpage><history><date date-type="received"><day>22</day><month>9</month><year>2005</year></date><date date-type="rev-recd"><day>28</day><month>10</month><year>2005</year></date><date date-type="accepted"><day>1</day><month>11</month><year>2005</year></date></history><permissions><copyright-statement>Copyright © 2005 Elsevier Ltd. All rights reserved.</copyright-statement><copyright-year>2005</copyright-year><copyright-holder>Elsevier Ltd</copyright-holder><license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p></license></permissions><abstract><p>Numerous human infections with avian influenza viruses in Asia in recent years have raised the concern that the next influenza pandemic is imminent. The most effective way to combat influenza is through the vaccination of the public. However, a minimum of 3–6 months is needed to develop an influenza vaccine using the traditional egg-based vaccine approach. The influenza hemagglutinin protein (HA), the active ingredient in the current vaccine, can be expressed in insect cells using the baculovirus expression vector system and purified rapidly. An influenza vaccine based on such a recombinant antigen allows a more timely response to a potential influenza pandemic. Here, we report an innovative monitoring assay for recombinant HA (rHA) expression and a rapid purification process. Various biochemical analyses indicate that the purified rHA is properly folded and biologically active.</p></abstract><kwd-group><title>Keywords</title><kwd>Influenza</kwd><kwd>Vaccine</kwd><kwd>Hemagglutinin</kwd><kwd>Baculovirus</kwd><kwd>Recombinant protein</kwd><kwd>Purification</kwd><kwd>Chromatography</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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