H2N2V1, 1957, Analysis, bibRecord, 000151

Early Alterations of the Receptor-Binding Properties of H1, H2, and H3 Avian Influenza Virus Hemagglutinins after Their Introduction into Mammals

Identifieur interne : 000151 ( 1957/Analysis ); précédent : 000150; suivant : 000152

Early Alterations of the Receptor-Binding Properties of H1, H2, and H3 Avian Influenza Virus Hemagglutinins after Their Introduction into Mammals

Auteurs : Mikhail Matrosovich ; Alexander Tuzikov ; Nikolai Bovin ; Alexandra Gambaryan ; Alexander Klimov ; Maria R. Castrucci ; Isabella Donatelli ; Yoshihiro Kawaoka [États-Unis]

Source :

Journal of Virology [ 0022-538X ] ; 2000.

RBID : PMC:116362

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Animals, Disease Outbreaks, Ducks (virology), Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Humans, Influenza A virus (isolation & purification), Influenza A virus (metabolism), Models, Molecular, Molecular Sequence Data, Mutation, Missense, Phylogeny, Protein Binding, Receptors, Virus (metabolism), Seals, Earless (virology), Sequence Alignment, Sialic Acids (metabolism), Species Specificity, Swine (virology).
MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Receptors, Virus, Sialic Acids.
- isolation & purification : Influenza A virus.
- metabolism : Influenza A virus.
- virology : Ducks, Seals, Earless, Swine.
- Amino Acid Sequence, Amino Acid Substitution, Animals, Disease Outbreaks, Humans, Models, Molecular, Molecular Sequence Data, Mutation, Missense, Phylogeny, Protein Binding, Sequence Alignment, Species Specificity.

Abstract

Interspecies transmission of influenza A viruses circulating in wild aquatic birds occasionally results in influenza outbreaks in mammals, including humans. To identify early changes in the receptor binding properties of the avian virus hemagglutinin (HA) after interspecies transmission and to determine the amino acid substitutions responsible for these alterations, we studied the HAs of the initial isolates from the human pandemics of 1957 (H2N2) and 1968 (H3N2), the European swine epizootic of 1979 (H1N1), and the seal epizootic of 1992 (H3N3), all of which were caused by the introduction of avian virus HAs into these species. The viruses were assayed for their ability to bind the synthetic sialylglycopolymers 3′SL-PAA and 6′SLN-PAA, which contained, respectively, 3′-sialyllactose (the receptor determinant preferentially recognized by avian influenza viruses) and 6′-sialyl(N-acetyllactosamine) (the receptor determinant for human viruses). Avian and seal viruses bound 6′SLN-PAA very weakly, whereas the earliest available human and swine epidemic viruses bound this polymer with a higher affinity. For the H2 and H3 strains, a single mutation, 226Q→L, increased binding to 6′SLN-PAA, while among H1 swine viruses, the 190E→D and 225G→E mutations in the HA appeared important for the increased affinity of the viruses for 6′SLN-PAA. Amino acid substitutions at positions 190 and 225 with respect to the avian virus consensus sequence are also present in H1 human viruses, including those that circulated in 1918, suggesting that substitutions at these positions are important for the generation of H1 human pandemic strains. These results show that the receptor-binding specificity of the HA is altered early after the transmission of an avian virus to humans and pigs and, therefore, may be a prerequisite for the highly effective replication and spread which characterize epidemic strains.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC116362

PubMed: 10954551
PubMed Central: 116362

Affiliations:

Links to Exploration step

PMC:116362

Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Early Alterations of the Receptor-Binding Properties of H1, H2, and H3 Avian Influenza Virus Hemagglutinins after  Their Introduction into Mammals</title>
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<series><title level="j">Journal of Virology</title>
<idno type="ISSN">0022-538X</idno>
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<term>Amino Acid Substitution</term>
<term>Animals</term>
<term>Disease Outbreaks</term>
<term>Ducks (virology)</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (chemistry)</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (metabolism)</term>
<term>Humans</term>
<term>Influenza A virus (isolation & purification)</term>
<term>Influenza A virus (metabolism)</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Mutation, Missense</term>
<term>Phylogeny</term>
<term>Protein Binding</term>
<term>Receptors, Virus (metabolism)</term>
<term>Seals, Earless (virology)</term>
<term>Sequence Alignment</term>
<term>Sialic Acids (metabolism)</term>
<term>Species Specificity</term>
<term>Swine (virology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acides sialiques (métabolisme)</term>
<term>Alignement de séquences</term>
<term>Animaux</term>
<term>Canards (virologie)</term>
<term>Données de séquences moléculaires</term>
<term>Flambées de maladies</term>
<term>Glycoprotéine hémagglutinine du virus influenza ()</term>
<term>Glycoprotéine hémagglutinine du virus influenza (métabolisme)</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Mutation faux-sens</term>
<term>Phoques (virologie)</term>
<term>Phylogénie</term>
<term>Récepteurs viraux (métabolisme)</term>
<term>Spécificité d'espèce</term>
<term>Substitution d'acide aminé</term>
<term>Suidae (virologie)</term>
<term>Séquence d'acides aminés</term>
<term>Virus de la grippe A (isolement et purification)</term>
<term>Virus de la grippe A (métabolisme)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term>
<term>Receptors, Virus</term>
<term>Sialic Acids</term>
</keywords>
<keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Influenza A virus</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Virus de la grippe A</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza A virus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides sialiques</term>
<term>Glycoprotéine hémagglutinine du virus influenza</term>
<term>Récepteurs viraux</term>
<term>Virus de la grippe A</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Canards</term>
<term>Phoques</term>
<term>Suidae</term>
</keywords>
<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Ducks</term>
<term>Seals, Earless</term>
<term>Swine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Amino Acid Substitution</term>
<term>Animals</term>
<term>Disease Outbreaks</term>
<term>Humans</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Mutation, Missense</term>
<term>Phylogeny</term>
<term>Protein Binding</term>
<term>Sequence Alignment</term>
<term>Species Specificity</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term>
<term>Animaux</term>
<term>Données de séquences moléculaires</term>
<term>Flambées de maladies</term>
<term>Glycoprotéine hémagglutinine du virus influenza</term>
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<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Mutation faux-sens</term>
<term>Phylogénie</term>
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<front><div type="abstract" xml:lang="en"><p>Interspecies transmission of influenza A viruses circulating in wild aquatic birds occasionally results in influenza outbreaks in mammals, including humans. To identify early changes in the receptor binding properties of the avian virus hemagglutinin (HA) after interspecies transmission and to determine the amino acid substitutions responsible for these alterations, we studied the HAs of the initial isolates from the human pandemics of 1957 (H2N2) and 1968 (H3N2), the European swine epizootic of 1979 (H1N1), and the seal epizootic of 1992 (H3N3), all of which were caused by the introduction of avian virus HAs into these species. The viruses were assayed for their ability to bind the synthetic sialylglycopolymers 3′SL-PAA and 6′SLN-PAA, which contained, respectively, 3′-sialyllactose (the receptor determinant preferentially recognized by avian influenza viruses) and 6′-sialyl(<italic>N</italic>
-acetyllactosamine) (the receptor determinant for human viruses). Avian and seal viruses bound 6′SLN-PAA very weakly, whereas the earliest available human and swine epidemic viruses bound this polymer with a higher affinity. For the H2 and H3 strains, a single mutation, 226Q→L, increased binding to 6′SLN-PAA, while among H1 swine viruses, the 190E→D and 225G→E mutations in the HA appeared important for the increased affinity of the viruses for 6′SLN-PAA. Amino acid substitutions at positions 190 and 225 with respect to the avian virus consensus sequence are also present in H1 human viruses, including those that circulated in 1918, suggesting that substitutions at these positions are important for the generation of H1 human pandemic strains. These results show that the receptor-binding specificity of the HA is altered early after the transmission of an avian virus to humans and pigs and, therefore, may be a prerequisite for the highly effective replication and spread which characterize epidemic strains.</p>
</div>
</front>
</TEI>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Wisconsin</li>
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<tree><noCountry><name sortKey="Bovin, Nikolai" sort="Bovin, Nikolai" uniqKey="Bovin N" first="Nikolai" last="Bovin">Nikolai Bovin</name>
<name sortKey="Castrucci, Maria R" sort="Castrucci, Maria R" uniqKey="Castrucci M" first="Maria R." last="Castrucci">Maria R. Castrucci</name>
<name sortKey="Donatelli, Isabella" sort="Donatelli, Isabella" uniqKey="Donatelli I" first="Isabella" last="Donatelli">Isabella Donatelli</name>
<name sortKey="Gambaryan, Alexandra" sort="Gambaryan, Alexandra" uniqKey="Gambaryan A" first="Alexandra" last="Gambaryan">Alexandra Gambaryan</name>
<name sortKey="Klimov, Alexander" sort="Klimov, Alexander" uniqKey="Klimov A" first="Alexander" last="Klimov">Alexander Klimov</name>
<name sortKey="Matrosovich, Mikhail" sort="Matrosovich, Mikhail" uniqKey="Matrosovich M" first="Mikhail" last="Matrosovich">Mikhail Matrosovich</name>
<name sortKey="Tuzikov, Alexander" sort="Tuzikov, Alexander" uniqKey="Tuzikov A" first="Alexander" last="Tuzikov">Alexander Tuzikov</name>
</noCountry>
<country name="États-Unis"><region name="Wisconsin"><name sortKey="Kawaoka, Yoshihiro" sort="Kawaoka, Yoshihiro" uniqKey="Kawaoka Y" first="Yoshihiro" last="Kawaoka">Yoshihiro Kawaoka</name>
</region>
<name sortKey="Kawaoka, Yoshihiro" sort="Kawaoka, Yoshihiro" uniqKey="Kawaoka Y" first="Yoshihiro" last="Kawaoka">Yoshihiro Kawaoka</name>
<name sortKey="Kawaoka, Yoshihiro" sort="Kawaoka, Yoshihiro" uniqKey="Kawaoka Y" first="Yoshihiro" last="Kawaoka">Yoshihiro Kawaoka</name>
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Early Alterations of the Receptor-Binding Properties of H1, H2, and H3 Avian Influenza Virus Hemagglutinins after Their Introduction into Mammals

Early Alterations of the Receptor-Binding Properties of H1, H2, and H3 Avian Influenza Virus Hemagglutinins after Their Introduction into Mammals

Source :

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Abstract

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