The matrix gene segment destabilizes the acid and thermal stability of the hemagglutinin of pandemic live attenuated influenza virus vaccines.
Identifieur interne : 000652 ( Main/Exploration ); précédent : 000651; suivant : 000653The matrix gene segment destabilizes the acid and thermal stability of the hemagglutinin of pandemic live attenuated influenza virus vaccines.
Auteurs : Christopher D. O'Donnell [États-Unis] ; Leatrice Vogel [États-Unis] ; Yumiko Matsuoka [États-Unis] ; Hong Jin [États-Unis] ; Kanta Subbarao [Indonésie]Source :
- Journal of virology [ 1098-5514 ] ; 2014.
Descripteurs français
- KwdFr :
- Concentration en ions d'hydrogène, Humains, Hémagglutinines (), Protéines de la matrice virale (génétique), Réplication virale (), Réplication virale (effets des radiations), Sous-type H1N1 du virus de la grippe A (), Sous-type H1N1 du virus de la grippe A (génétique), Sous-type H1N1 du virus de la grippe A (physiologie), Stabilité de médicament, Stabilité protéique (), Stabilité protéique (effets des radiations), Température, Vaccins antigrippaux (), Vaccins antigrippaux (génétique), Vaccins atténués (), Vaccins atténués (génétique), Virus recombinants (), Virus recombinants (génétique), Virus recombinants (physiologie).
- MESH :
- effets des radiations : Réplication virale, Stabilité protéique.
- génétique : Protéines de la matrice virale, Sous-type H1N1 du virus de la grippe A, Vaccins antigrippaux, Vaccins atténués, Virus recombinants.
- physiologie : Sous-type H1N1 du virus de la grippe A, Virus recombinants.
- Concentration en ions d'hydrogène, Humains, Hémagglutinines, Réplication virale, Sous-type H1N1 du virus de la grippe A, Stabilité de médicament, Stabilité protéique, Température, Vaccins antigrippaux, Vaccins atténués, Virus recombinants.
English descriptors
- KwdEn :
- Drug Stability, Hemagglutinins (chemistry), Humans, Hydrogen-Ion Concentration, Influenza A Virus, H1N1 Subtype (chemistry), Influenza A Virus, H1N1 Subtype (genetics), Influenza A Virus, H1N1 Subtype (physiology), Influenza Vaccines (chemistry), Influenza Vaccines (genetics), Protein Stability (drug effects), Protein Stability (radiation effects), Reassortant Viruses (chemistry), Reassortant Viruses (genetics), Reassortant Viruses (physiology), Temperature, Vaccines, Attenuated (chemistry), Vaccines, Attenuated (genetics), Viral Matrix Proteins (genetics), Virus Replication (drug effects), Virus Replication (radiation effects).
- MESH :
- chemical , chemistry : Hemagglutinins, Influenza Vaccines, Vaccines, Attenuated.
- chemistry : Influenza A Virus, H1N1 Subtype, Reassortant Viruses.
- drug effects : Protein Stability, Virus Replication.
- genetics : Influenza A Virus, H1N1 Subtype, Influenza Vaccines, Reassortant Viruses, Vaccines, Attenuated, Viral Matrix Proteins.
- physiology : Influenza A Virus, H1N1 Subtype, Reassortant Viruses.
- radiation effects : Protein Stability, Virus Replication.
- Drug Stability, Humans, Hydrogen-Ion Concentration, Temperature.
Abstract
The threat of future influenza pandemics and their potential for rapid spread, morbidity, and mortality has led to the development of pandemic vaccines. We generated seven reassortant pandemic live attenuated influenza vaccines (pLAIVs) with the hemagglutinin (HA) and neuraminidase (NA) genes derived from animal influenza viruses on the backbone of the six internal protein gene segments of the temperature sensitive, cold-adapted (ca) A/Ann Arbor/60 (H2N2) virus (AA/60 ca) of the licensed seasonal LAIV. The pLAIV viruses were moderately to highly restricted in replication in seronegative adults; we sought to determine the biological basis for this restriction. Avian influenza viruses generally replicate at higher temperatures than human influenza viruses and, although they shared the same backbone, the pLAIV viruses had a lower shutoff temperature than seasonal LAIV viruses, suggesting that the HA and NA influence the degree of temperature sensitivity. The pH of HA activation of highly pathogenic avian influenza viruses was greater than human and low-pathogenicity avian influenza viruses, as reported by others. However, pLAIV viruses had a consistently higher pH of HA activation and reduced HA thermostability compared to the corresponding wild-type parental viruses. From studies with single-gene reassortant viruses bearing one gene segment from the AA/60 ca virus in recombinant H5N1 or pH1N1 viruses, we found that the lower HA thermal stability and increased pH of HA activation were associated with the AA/60 M gene. Together, the impaired HA acid and thermal stability and temperature sensitivity likely contributed to the restricted replication of the pLAIV viruses we observed in seronegative adults.
DOI: 10.1128/JVI.01107-14
PubMed: 25122789
Affiliations:
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Infectious Diseases, NIAID, NIH, Bethesda, Maryland, USA ksubbarao@niaid.nih.gov.</nlm:affiliation><country wicri:rule="url">Indonésie</country><wicri:regionArea>Laboratory of Infectious Diseases, NIAID, NIH, Bethesda, Maryland</wicri:regionArea><wicri:noRegion>Maryland</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Drug Stability</term><term>Hemagglutinins (chemistry)</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Influenza A Virus, H1N1 Subtype (chemistry)</term><term>Influenza A Virus, H1N1 Subtype (genetics)</term><term>Influenza A Virus, H1N1 Subtype (physiology)</term><term>Influenza Vaccines (chemistry)</term><term>Influenza Vaccines (genetics)</term><term>Protein Stability (drug effects)</term><term>Protein Stability (radiation effects)</term><term>Reassortant Viruses (chemistry)</term><term>Reassortant Viruses (genetics)</term><term>Reassortant Viruses (physiology)</term><term>Temperature</term><term>Vaccines, Attenuated (chemistry)</term><term>Vaccines, Attenuated (genetics)</term><term>Viral Matrix Proteins (genetics)</term><term>Virus Replication (drug effects)</term><term>Virus Replication (radiation effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Humains</term><term>Hémagglutinines ()</term><term>Protéines de la matrice virale (génétique)</term><term>Réplication virale ()</term><term>Réplication virale (effets des radiations)</term><term>Sous-type H1N1 du virus de la grippe A ()</term><term>Sous-type H1N1 du virus de la grippe A (génétique)</term><term>Sous-type H1N1 du virus de la grippe A (physiologie)</term><term>Stabilité de médicament</term><term>Stabilité protéique ()</term><term>Stabilité protéique (effets des radiations)</term><term>Température</term><term>Vaccins antigrippaux ()</term><term>Vaccins antigrippaux (génétique)</term><term>Vaccins atténués ()</term><term>Vaccins atténués (génétique)</term><term>Virus recombinants ()</term><term>Virus recombinants (génétique)</term><term>Virus recombinants (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinins</term><term>Influenza Vaccines</term><term>Vaccines, Attenuated</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term><term>Reassortant Viruses</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Protein Stability</term><term>Virus Replication</term></keywords><keywords scheme="MESH" qualifier="effets des radiations" xml:lang="fr"><term>Réplication virale</term><term>Stabilité protéique</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term><term>Influenza Vaccines</term><term>Reassortant Viruses</term><term>Vaccines, Attenuated</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de la matrice virale</term><term>Sous-type H1N1 du virus de la grippe A</term><term>Vaccins antigrippaux</term><term>Vaccins atténués</term><term>Virus recombinants</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Sous-type H1N1 du virus de la grippe A</term><term>Virus recombinants</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term><term>Reassortant Viruses</term></keywords><keywords scheme="MESH" qualifier="radiation effects" xml:lang="en"><term>Protein Stability</term><term>Virus Replication</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Drug Stability</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Humains</term><term>Hémagglutinines</term><term>Réplication virale</term><term>Sous-type H1N1 du virus de la grippe A</term><term>Stabilité de médicament</term><term>Stabilité protéique</term><term>Température</term><term>Vaccins antigrippaux</term><term>Vaccins atténués</term><term>Virus recombinants</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The threat of future influenza pandemics and their potential for rapid spread, morbidity, and mortality has led to the development of pandemic vaccines. We generated seven reassortant pandemic live attenuated influenza vaccines (pLAIVs) with the hemagglutinin (HA) and neuraminidase (NA) genes derived from animal influenza viruses on the backbone of the six internal protein gene segments of the temperature sensitive, cold-adapted (ca) A/Ann Arbor/60 (H2N2) virus (AA/60 ca) of the licensed seasonal LAIV. The pLAIV viruses were moderately to highly restricted in replication in seronegative adults; we sought to determine the biological basis for this restriction. Avian influenza viruses generally replicate at higher temperatures than human influenza viruses and, although they shared the same backbone, the pLAIV viruses had a lower shutoff temperature than seasonal LAIV viruses, suggesting that the HA and NA influence the degree of temperature sensitivity. The pH of HA activation of highly pathogenic avian influenza viruses was greater than human and low-pathogenicity avian influenza viruses, as reported by others. However, pLAIV viruses had a consistently higher pH of HA activation and reduced HA thermostability compared to the corresponding wild-type parental viruses. From studies with single-gene reassortant viruses bearing one gene segment from the AA/60 ca virus in recombinant H5N1 or pH1N1 viruses, we found that the lower HA thermal stability and increased pH of HA activation were associated with the AA/60 M gene. Together, the impaired HA acid and thermal stability and temperature sensitivity likely contributed to the restricted replication of the pLAIV viruses we observed in seronegative adults.</div></front></TEI><affiliations><list><country><li>Indonésie</li><li>États-Unis</li></country><region><li>Californie</li><li>Maryland</li></region></list><tree><country name="États-Unis"><region name="Maryland"><name sortKey="O Donnell, Christopher D" sort="O Donnell, Christopher D" uniqKey="O Donnell C" first="Christopher D" last="O'Donnell">Christopher D. O'Donnell</name></region><name sortKey="Jin, Hong" sort="Jin, Hong" uniqKey="Jin H" first="Hong" last="Jin">Hong Jin</name><name sortKey="Matsuoka, Yumiko" sort="Matsuoka, Yumiko" uniqKey="Matsuoka Y" first="Yumiko" last="Matsuoka">Yumiko Matsuoka</name><name sortKey="Vogel, Leatrice" sort="Vogel, Leatrice" uniqKey="Vogel L" first="Leatrice" last="Vogel">Leatrice Vogel</name></country><country name="Indonésie"><noRegion><name sortKey="Subbarao, Kanta" sort="Subbarao, Kanta" uniqKey="Subbarao K" first="Kanta" last="Subbarao">Kanta Subbarao</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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