H5 N-terminal β sheet promotes oligomerization of H7-HA1 that induces better antibody affinity maturation and enhanced protection against H7N7 and H7N9 viruses compared to inactivated influenza vaccine.
Identifieur interne : 000E53 ( Main/Exploration ); précédent : 000E52; suivant : 000E54H5 N-terminal β sheet promotes oligomerization of H7-HA1 that induces better antibody affinity maturation and enhanced protection against H7N7 and H7N9 viruses compared to inactivated influenza vaccine.
Auteurs : Surender Khurana [États-Unis] ; Elizabeth M. Coyle [États-Unis] ; Swati Verma [États-Unis] ; Lisa R. King [États-Unis] ; Jody Manischewitz [États-Unis] ; Corey J. Crevar [États-Unis] ; Donald M. Carter [États-Unis] ; Ted M. Ross [États-Unis] ; Hana Golding [États-Unis]Source :
- Vaccine [ 1873-2518 ] ; 2014.
Descripteurs français
- KwdFr :
- Affinité des anticorps (immunologie), Animaux, Anticorps antiviraux (sang), Anticorps neutralisants (sang), Femelle, Furets, Glycoprotéine hémagglutinine du virus influenza (immunologie), Humains, Infections à Orthomyxoviridae (), Lapins, Multimérisation de protéines, Sous-type H5N1 du virus de la grippe A, Sous-type H7N7 du virus de la grippe A, Sous-type H7N9 du virus de la grippe A, Structure tertiaire des protéines, Tests d'hémagglutination, Vaccins antigrippaux (immunologie), Vaccins inactivés (immunologie).
- MESH :
- immunologie : Affinité des anticorps, Glycoprotéine hémagglutinine du virus influenza, Vaccins antigrippaux, Vaccins inactivés.
- sang : Anticorps antiviraux, Anticorps neutralisants.
- Animaux, Femelle, Furets, Humains, Infections à Orthomyxoviridae, Lapins, Multimérisation de protéines, Sous-type H5N1 du virus de la grippe A, Sous-type H7N7 du virus de la grippe A, Sous-type H7N9 du virus de la grippe A, Structure tertiaire des protéines, Tests d'hémagglutination.
English descriptors
- KwdEn :
- Animals, Antibodies, Neutralizing (blood), Antibodies, Viral (blood), Antibody Affinity (immunology), Female, Ferrets, Hemagglutination Tests, Hemagglutinin Glycoproteins, Influenza Virus (immunology), Humans, Influenza A Virus, H5N1 Subtype, Influenza A Virus, H7N7 Subtype, Influenza A Virus, H7N9 Subtype, Influenza Vaccines (immunology), Orthomyxoviridae Infections (prevention & control), Protein Multimerization, Protein Structure, Tertiary, Rabbits, Vaccines, Inactivated (immunology).
- MESH :
- chemical , blood : Antibodies, Neutralizing, Antibodies, Viral.
- immunology : Antibody Affinity, Hemagglutinin Glycoproteins, Influenza Virus, Influenza Vaccines, Vaccines, Inactivated.
- prevention & control : Orthomyxoviridae Infections.
- Animals, Female, Ferrets, Hemagglutination Tests, Humans, Influenza A Virus, H5N1 Subtype, Influenza A Virus, H7N7 Subtype, Influenza A Virus, H7N9 Subtype, Protein Multimerization, Protein Structure, Tertiary, Rabbits.
Abstract
Initiation of mass vaccination is critical in response to influenza pandemic. There is an urgent need of a simple, rapid method for production of influenza vaccine that is more effective than current traditional influenza vaccines. Recent H7N9 transmissions to humans in China with high morbidity/mortality initiated extensive vaccine evaluation. We produced the HA1 domains (amino acids 1-320) from H7N9 and H7N7 strains in E. coli. Both were found to contain primarily monomers/trimers with low oligomeric content. However, when residues from the N-terminal β sheet (first 8 amino acid) of H7 HA1 domains were swapped with the corresponding amino acids from H5N1, functional oligomeric H7 HA1 were produced (HA1-DS), demonstrating strong receptor binding and hemagglutination. In rabbits, the HA1-DS from either H7N9 or H7N7 generated high neutralization titers against both homologous and heterologous H7 strains, superior to the unmodified H7 HA1 proteins. In ferrets, HA1-DS from H7N7 elicited higher (and faster) HI titers, better protected ferrets from lethality, weight loss, and reduced viral loads following challenge with wild-type highly pathogenic H7N7 virus compared with inactivated H7N7 subunit vaccine. HA1-DS vaccinated ferrets were also better protected from weight loss after challenge with the heterologous H7N9 virus compared with inactivated H7N7 subunit vaccine. Importantly, the H7N7 HA1-DS vaccine induced antibody affinity maturation far superior to the inactivated H7N7 subunit vaccine, which strongly correlated with control of viral loads in the nasal washes after challenge with either H7N7 or H7N9 strains. We conclude that N-terminus β sheet domain-swap can be used to produce stable functional oligomeric forms of better recombinant HA1 vaccines in simple, inexpensive bacterial system for rapid response to emerging pandemic threat for the global population.
DOI: 10.1016/j.vaccine.2014.09.049
PubMed: 25284811
Affiliations:
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Le document en format XML
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Electronic address: Surender.Khurana@fda.hhs.gov.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Coyle, Elizabeth M" sort="Coyle, Elizabeth M" uniqKey="Coyle E" first="Elizabeth M" last="Coyle">Elizabeth M. Coyle</name><affiliation wicri:level="2"><nlm:affiliation>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Verma, Swati" sort="Verma, Swati" uniqKey="Verma S" first="Swati" last="Verma">Swati Verma</name><affiliation wicri:level="2"><nlm:affiliation>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="King, Lisa R" sort="King, Lisa R" uniqKey="King L" first="Lisa R" last="King">Lisa R. King</name><affiliation wicri:level="2"><nlm:affiliation>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Manischewitz, Jody" sort="Manischewitz, Jody" uniqKey="Manischewitz J" first="Jody" last="Manischewitz">Jody Manischewitz</name><affiliation wicri:level="2"><nlm:affiliation>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Crevar, Corey J" sort="Crevar, Corey J" uniqKey="Crevar C" first="Corey J" last="Crevar">Corey J. Crevar</name><affiliation wicri:level="1"><nlm:affiliation>Vaccine and Gene Therapy Institute of Florida, Miami, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Vaccine and Gene Therapy Institute of Florida, Miami</wicri:regionArea><wicri:noRegion>Miami</wicri:noRegion></affiliation></author><author><name sortKey="Carter, Donald M" sort="Carter, Donald M" uniqKey="Carter D" first="Donald M" last="Carter">Donald M. Carter</name><affiliation wicri:level="1"><nlm:affiliation>Vaccine and Gene Therapy Institute of Florida, Miami, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Vaccine and Gene Therapy Institute of Florida, Miami</wicri:regionArea><wicri:noRegion>Miami</wicri:noRegion></affiliation></author><author><name sortKey="Ross, Ted M" sort="Ross, Ted M" uniqKey="Ross T" first="Ted M" last="Ross">Ted M. Ross</name><affiliation wicri:level="1"><nlm:affiliation>Vaccine and Gene Therapy Institute of Florida, Miami, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Vaccine and Gene Therapy Institute of Florida, Miami</wicri:regionArea><wicri:noRegion>Miami</wicri:noRegion></affiliation></author><author><name sortKey="Golding, Hana" sort="Golding, Hana" uniqKey="Golding H" first="Hana" last="Golding">Hana Golding</name><affiliation wicri:level="2"><nlm:affiliation>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903, USA. Electronic address: Hana.Golding@fda.hhs.gov.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Division of Viral Products, Center for Biologics Evaluation and Research (CBER), Food and Drug Administration, Silver Spring, MD 20903</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author></analytic><series><title level="j">Vaccine</title><idno type="eISSN">1873-2518</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Neutralizing (blood)</term><term>Antibodies, Viral (blood)</term><term>Antibody Affinity (immunology)</term><term>Female</term><term>Ferrets</term><term>Hemagglutination Tests</term><term>Hemagglutinin Glycoproteins, Influenza Virus (immunology)</term><term>Humans</term><term>Influenza A Virus, H5N1 Subtype</term><term>Influenza A Virus, H7N7 Subtype</term><term>Influenza A Virus, H7N9 Subtype</term><term>Influenza Vaccines (immunology)</term><term>Orthomyxoviridae Infections (prevention & control)</term><term>Protein Multimerization</term><term>Protein Structure, Tertiary</term><term>Rabbits</term><term>Vaccines, Inactivated (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Affinité des anticorps (immunologie)</term><term>Animaux</term><term>Anticorps antiviraux (sang)</term><term>Anticorps neutralisants (sang)</term><term>Femelle</term><term>Furets</term><term>Glycoprotéine hémagglutinine du virus influenza (immunologie)</term><term>Humains</term><term>Infections à Orthomyxoviridae ()</term><term>Lapins</term><term>Multimérisation de protéines</term><term>Sous-type H5N1 du virus de la grippe A</term><term>Sous-type H7N7 du virus de la grippe A</term><term>Sous-type H7N9 du virus de la grippe A</term><term>Structure tertiaire des protéines</term><term>Tests d'hémagglutination</term><term>Vaccins antigrippaux (immunologie)</term><term>Vaccins inactivés (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="blood" xml:lang="en"><term>Antibodies, Neutralizing</term><term>Antibodies, Viral</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Affinité des anticorps</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Vaccins antigrippaux</term><term>Vaccins inactivés</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Antibody Affinity</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Influenza Vaccines</term><term>Vaccines, Inactivated</term></keywords><keywords scheme="MESH" qualifier="prevention & control" xml:lang="en"><term>Orthomyxoviridae Infections</term></keywords><keywords scheme="MESH" qualifier="sang" xml:lang="fr"><term>Anticorps antiviraux</term><term>Anticorps neutralisants</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Female</term><term>Ferrets</term><term>Hemagglutination Tests</term><term>Humans</term><term>Influenza A Virus, H5N1 Subtype</term><term>Influenza A Virus, H7N7 Subtype</term><term>Influenza A Virus, H7N9 Subtype</term><term>Protein Multimerization</term><term>Protein Structure, Tertiary</term><term>Rabbits</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Femelle</term><term>Furets</term><term>Humains</term><term>Infections à Orthomyxoviridae</term><term>Lapins</term><term>Multimérisation de protéines</term><term>Sous-type H5N1 du virus de la grippe A</term><term>Sous-type H7N7 du virus de la grippe A</term><term>Sous-type H7N9 du virus de la grippe A</term><term>Structure tertiaire des protéines</term><term>Tests d'hémagglutination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Initiation of mass vaccination is critical in response to influenza pandemic. There is an urgent need of a simple, rapid method for production of influenza vaccine that is more effective than current traditional influenza vaccines. Recent H7N9 transmissions to humans in China with high morbidity/mortality initiated extensive vaccine evaluation. We produced the HA1 domains (amino acids 1-320) from H7N9 and H7N7 strains in E. coli. Both were found to contain primarily monomers/trimers with low oligomeric content. However, when residues from the N-terminal β sheet (first 8 amino acid) of H7 HA1 domains were swapped with the corresponding amino acids from H5N1, functional oligomeric H7 HA1 were produced (HA1-DS), demonstrating strong receptor binding and hemagglutination. In rabbits, the HA1-DS from either H7N9 or H7N7 generated high neutralization titers against both homologous and heterologous H7 strains, superior to the unmodified H7 HA1 proteins. In ferrets, HA1-DS from H7N7 elicited higher (and faster) HI titers, better protected ferrets from lethality, weight loss, and reduced viral loads following challenge with wild-type highly pathogenic H7N7 virus compared with inactivated H7N7 subunit vaccine. HA1-DS vaccinated ferrets were also better protected from weight loss after challenge with the heterologous H7N9 virus compared with inactivated H7N7 subunit vaccine. Importantly, the H7N7 HA1-DS vaccine induced antibody affinity maturation far superior to the inactivated H7N7 subunit vaccine, which strongly correlated with control of viral loads in the nasal washes after challenge with either H7N7 or H7N9 strains. We conclude that N-terminus β sheet domain-swap can be used to produce stable functional oligomeric forms of better recombinant HA1 vaccines in simple, inexpensive bacterial system for rapid response to emerging pandemic threat for the global population. </div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><country name="États-Unis"><region name="Maryland"><name sortKey="Khurana, Surender" sort="Khurana, Surender" uniqKey="Khurana S" first="Surender" last="Khurana">Surender Khurana</name></region><name sortKey="Carter, Donald M" sort="Carter, Donald M" uniqKey="Carter D" first="Donald M" last="Carter">Donald M. Carter</name><name sortKey="Coyle, Elizabeth M" sort="Coyle, Elizabeth M" uniqKey="Coyle E" first="Elizabeth M" last="Coyle">Elizabeth M. Coyle</name><name sortKey="Crevar, Corey J" sort="Crevar, Corey J" uniqKey="Crevar C" first="Corey J" last="Crevar">Corey J. Crevar</name><name sortKey="Golding, Hana" sort="Golding, Hana" uniqKey="Golding H" first="Hana" last="Golding">Hana Golding</name><name sortKey="King, Lisa R" sort="King, Lisa R" uniqKey="King L" first="Lisa R" last="King">Lisa R. King</name><name sortKey="Manischewitz, Jody" sort="Manischewitz, Jody" uniqKey="Manischewitz J" first="Jody" last="Manischewitz">Jody Manischewitz</name><name sortKey="Ross, Ted M" sort="Ross, Ted M" uniqKey="Ross T" first="Ted M" last="Ross">Ted M. Ross</name><name sortKey="Verma, Swati" sort="Verma, Swati" uniqKey="Verma S" first="Swati" last="Verma">Swati Verma</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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