Contribution of antibody production against neuraminidase to the protection afforded by influenza vaccines
Identifieur interne : 000B31 ( Main/Exploration ); précédent : 000B30; suivant : 000B32Contribution of antibody production against neuraminidase to the protection afforded by influenza vaccines
Auteurs : Glendie Marcelin [États-Unis] ; Matthew R. Sandbulte [États-Unis] ; Richard J. Webby [États-Unis]Source :
- Reviews in Medical Virology [ 1052-9276 ] ; 2012-07.
English descriptors
- Teeft :
- Amino acids, Animal models, Animal studies, Annual review, Antibody, Antibody response, Antibody responses, Antibody titers, Antigenic, Antigenic characteristics, Antigenic competition, Antigenic drift, Antigenic sites, Antigenically, Assay, Avian, Avian diseases, Avian virus, Baculovirus vector, Catalytic site, Clinical data, Clinical trials, Conventional vaccines, Copyright, Disease severity, Divalent cation requirements, England journal, Enzymatic activity, Fetuin, Functional antibodies, Globular head, Glycoprotein, Hemagglutinin, Host cells, Human population, Immune, Immune response, Immune responses, Immunity, Immunization, Immunogenicity, Immunological methods, Immunosorbent assay, Infection, Infectious diseases, Johansson, John wiley sons, Jude research hospital, Kilbourne, Laver, Many years, Marcelin, Monoclonal antibodies, Nascent virions, National academy, Natural exposure, Natural infection, Neuraminidase, Neuraminidase antibodies, Neuraminidase antibody, Neuraminidase antibody responses, Neuraminidase protein, Neutralizing antibodies, Pandemic, Partial protection, Peanut agglutinin lectin, Plo, Protective immunity, Recombinant, Replication, Seasonal, Seasonal vaccine, Seasonal vaccine strains, Seasonal vaccines, Seasonal viruses, Serum antibodies, Sialic, Sialic acid, Surface antigens, Thiobarbituric acid, Trivalent, Unprimed populations, Vaccine, Vaccine formulations, Vaccine preparation, Vaccine strain, Vaccine technologies, Viral, Viral particles, Viral replication, Virion, Virol, Virology, Virology journal, Virus, Virus challenge, Virus hemagglutinin, Virus infection, Virus neuraminidase, Virus neuraminidases, Virus replication, Whole virions, Young children.
Abstract
Vaccines are instrumental in controlling the burden of influenza virus infection in humans and animals. Antibodies raised against both major viral surface glycoproteins, hemagglutinin (HA) and neuraminidase (NA), can contribute to protective immunity. Vaccine‐induced HA antibodies have been characterized extensively, and they generally confer protection by blocking the attachment and fusion of a homologous virus onto host cells. Although not as well characterized, some functions of NA antibodies in influenza vaccine‐mediated immunity have been recognized for many years. In this review, we summarize the case for NA antibodies in influenza vaccine‐mediated immunity. In the absence of well‐matched HA antibodies, NA antibodies can provide varying degrees of protection against disease. NA proteins of seasonal influenza vaccines have been shown in some instances to elicit serum antibodies with cross‐reactivity to avian‐origin and swine‐origin influenza strains, in addition to HA drift variants. NA‐mediated immunity has been linked to (i) conserved NA epitopes amongst otherwise antigenically distinct strains, partly attributable to the segmented influenza viral genome; (ii) inhibition of NA enzymatic activity; and (iii) the NA content in vaccine formulations. There is a potential to enhance the effectiveness of existing and future influenza vaccines by focusing greater attention on the antigenic characteristics and potency of the NA protein. Copyright © 2012 John Wiley & Sons, Ltd.
Url:
DOI: 10.1002/rmv.1713
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 001469
- to stream Istex, to step Curation: 001469
- to stream Istex, to step Checkpoint: 000108
- to stream Main, to step Merge: 000B34
- to stream Main, to step Curation: 000B31
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Contribution of antibody production against neuraminidase to the protection afforded by influenza vaccines</title><author><name sortKey="Marcelin, Glendie" sort="Marcelin, Glendie" uniqKey="Marcelin G" first="Glendie" last="Marcelin">Glendie Marcelin</name></author><author><name sortKey="Sandbulte, Matthew R" sort="Sandbulte, Matthew R" uniqKey="Sandbulte M" first="Matthew R." last="Sandbulte">Matthew R. Sandbulte</name></author><author><name sortKey="Webby, Richard J" sort="Webby, Richard J" uniqKey="Webby R" first="Richard J." last="Webby">Richard J. Webby</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:37E2899484586B876C4929FA2BF8F61331AD9379</idno><date when="2012" year="2012">2012</date><idno type="doi">10.1002/rmv.1713</idno><idno type="url">https://api.istex.fr/ark:/67375/WNG-95DFQTQ6-W/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001469</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001469</idno><idno type="wicri:Area/Istex/Curation">001469</idno><idno type="wicri:Area/Istex/Checkpoint">000108</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000108</idno><idno type="wicri:doubleKey">1052-9276:2012:Marcelin G:contribution:of:antibody</idno><idno type="wicri:Area/Main/Merge">000B34</idno><idno type="wicri:Area/Main/Curation">000B31</idno><idno type="wicri:Area/Main/Exploration">000B31</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Contribution of antibody production against neuraminidase to the protection afforded by influenza vaccines</title><author><name sortKey="Marcelin, Glendie" sort="Marcelin, Glendie" uniqKey="Marcelin G" first="Glendie" last="Marcelin">Glendie Marcelin</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Infectious Diseases, Division Virology, St. Jude Children's Research Hospital, TN, Memphis</wicri:regionArea><wicri:noRegion>Memphis</wicri:noRegion></affiliation></author><author><name sortKey="Sandbulte, Matthew R" sort="Sandbulte, Matthew R" uniqKey="Sandbulte M" first="Matthew R." last="Sandbulte">Matthew R. Sandbulte</name><affiliation wicri:level="4"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Veterinary Microbiology and Preventive Medicine, Iowa State University, IA, Ames</wicri:regionArea><orgName type="university">Université d'État de l'Iowa</orgName><placeName><settlement type="city">Ames (Iowa)</settlement><region type="state">Iowa</region></placeName></affiliation></author><author><name sortKey="Webby, Richard J" sort="Webby, Richard J" uniqKey="Webby R" first="Richard J." last="Webby">Richard J. Webby</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Infectious Diseases, Division Virology, St. Jude Children's Research Hospital, TN, Memphis</wicri:regionArea><wicri:noRegion>Memphis</wicri:noRegion></affiliation><affiliation></affiliation><affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Reviews in Medical Virology</title><title level="j" type="alt">REVIEWS IN MEDICAL VIROLOGY</title><idno type="ISSN">1052-9276</idno><idno type="eISSN">1099-1654</idno><imprint><biblScope unit="vol">22</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="267">267</biblScope><biblScope unit="page" to="279">279</biblScope><biblScope unit="page-count">13</biblScope><publisher>John Wiley & Sons, Ltd</publisher><pubPlace>Chichester, UK</pubPlace><date type="published" when="2012-07">2012-07</date></imprint><idno type="ISSN">1052-9276</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1052-9276</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino acids</term><term>Animal models</term><term>Animal studies</term><term>Annual review</term><term>Antibody</term><term>Antibody response</term><term>Antibody responses</term><term>Antibody titers</term><term>Antigenic</term><term>Antigenic characteristics</term><term>Antigenic competition</term><term>Antigenic drift</term><term>Antigenic sites</term><term>Antigenically</term><term>Assay</term><term>Avian</term><term>Avian diseases</term><term>Avian virus</term><term>Baculovirus vector</term><term>Catalytic site</term><term>Clinical data</term><term>Clinical trials</term><term>Conventional vaccines</term><term>Copyright</term><term>Disease severity</term><term>Divalent cation requirements</term><term>England journal</term><term>Enzymatic activity</term><term>Fetuin</term><term>Functional antibodies</term><term>Globular head</term><term>Glycoprotein</term><term>Hemagglutinin</term><term>Host cells</term><term>Human population</term><term>Immune</term><term>Immune response</term><term>Immune responses</term><term>Immunity</term><term>Immunization</term><term>Immunogenicity</term><term>Immunological methods</term><term>Immunosorbent assay</term><term>Infection</term><term>Infectious diseases</term><term>Johansson</term><term>John wiley sons</term><term>Jude research hospital</term><term>Kilbourne</term><term>Laver</term><term>Many years</term><term>Marcelin</term><term>Monoclonal antibodies</term><term>Nascent virions</term><term>National academy</term><term>Natural exposure</term><term>Natural infection</term><term>Neuraminidase</term><term>Neuraminidase antibodies</term><term>Neuraminidase antibody</term><term>Neuraminidase antibody responses</term><term>Neuraminidase protein</term><term>Neutralizing antibodies</term><term>Pandemic</term><term>Partial protection</term><term>Peanut agglutinin lectin</term><term>Plo</term><term>Protective immunity</term><term>Recombinant</term><term>Replication</term><term>Seasonal</term><term>Seasonal vaccine</term><term>Seasonal vaccine strains</term><term>Seasonal vaccines</term><term>Seasonal viruses</term><term>Serum antibodies</term><term>Sialic</term><term>Sialic acid</term><term>Surface antigens</term><term>Thiobarbituric acid</term><term>Trivalent</term><term>Unprimed populations</term><term>Vaccine</term><term>Vaccine formulations</term><term>Vaccine preparation</term><term>Vaccine strain</term><term>Vaccine technologies</term><term>Viral</term><term>Viral particles</term><term>Viral replication</term><term>Virion</term><term>Virol</term><term>Virology</term><term>Virology journal</term><term>Virus</term><term>Virus challenge</term><term>Virus hemagglutinin</term><term>Virus infection</term><term>Virus neuraminidase</term><term>Virus neuraminidases</term><term>Virus replication</term><term>Whole virions</term><term>Young children</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract">Vaccines are instrumental in controlling the burden of influenza virus infection in humans and animals. Antibodies raised against both major viral surface glycoproteins, hemagglutinin (HA) and neuraminidase (NA), can contribute to protective immunity. Vaccine‐induced HA antibodies have been characterized extensively, and they generally confer protection by blocking the attachment and fusion of a homologous virus onto host cells. Although not as well characterized, some functions of NA antibodies in influenza vaccine‐mediated immunity have been recognized for many years. In this review, we summarize the case for NA antibodies in influenza vaccine‐mediated immunity. In the absence of well‐matched HA antibodies, NA antibodies can provide varying degrees of protection against disease. NA proteins of seasonal influenza vaccines have been shown in some instances to elicit serum antibodies with cross‐reactivity to avian‐origin and swine‐origin influenza strains, in addition to HA drift variants. NA‐mediated immunity has been linked to (i) conserved NA epitopes amongst otherwise antigenically distinct strains, partly attributable to the segmented influenza viral genome; (ii) inhibition of NA enzymatic activity; and (iii) the NA content in vaccine formulations. There is a potential to enhance the effectiveness of existing and future influenza vaccines by focusing greater attention on the antigenic characteristics and potency of the NA protein. Copyright © 2012 John Wiley & Sons, Ltd.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Iowa</li></region><settlement><li>Ames (Iowa)</li></settlement><orgName><li>Université d'État de l'Iowa</li></orgName></list><tree><country name="États-Unis"><noRegion><name sortKey="Marcelin, Glendie" sort="Marcelin, Glendie" uniqKey="Marcelin G" first="Glendie" last="Marcelin">Glendie Marcelin</name></noRegion><name sortKey="Sandbulte, Matthew R" sort="Sandbulte, Matthew R" uniqKey="Sandbulte M" first="Matthew R." last="Sandbulte">Matthew R. Sandbulte</name><name sortKey="Webby, Richard J" sort="Webby, Richard J" uniqKey="Webby R" first="Richard J." last="Webby">Richard J. Webby</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000B31 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000B31 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Main
|étape= Exploration
|type= RBID
|clé= ISTEX:37E2899484586B876C4929FA2BF8F61331AD9379
|texte= Contribution of antibody production against neuraminidase to the protection afforded by influenza vaccines
}}
| This area was generated with Dilib version V0.6.33. |  |