H2N2V1, 1957, Analysis, bibRecord, 000144

Amino Acids Responsible for the Absolute Sialidase Activity of the Influenza A Virus Neuraminidase: Relationship to Growth in the Duck Intestine

Identifieur interne : 000144 ( 1957/Analysis ); précédent : 000143; suivant : 000145

Amino Acids Responsible for the Absolute Sialidase Activity of the Influenza A Virus Neuraminidase: Relationship to Growth in the Duck Intestine

Auteurs : Darwyn Kobasa ; Krisna Wells ; Yoshihiro Kawaoka [États-Unis]

Source :

Journal of Virology [ 0022-538X ] ; 2001.

RBID : PMC:114763

Descripteurs français

KwdFr :
- Amorces ADN, Animaux, Canards, Intestins (virologie), Modèles moléculaires, Mutagenèse dirigée, Réplication virale, Sialidase (), Sialidase (génétique), Sialidase (métabolisme), Substitution d'acide aminé, Séquence nucléotidique, Virus de la grippe A (croissance et développement), Virus de la grippe A (enzymologie), Virus de la grippe A (physiologie), Virus recombinants (croissance et développement), Virus recombinants (enzymologie), Virus recombinants (génétique), Virus recombinants (physiologie).
MESH :
- croissance et développement : Virus de la grippe A, Virus recombinants.
- enzymologie : Virus de la grippe A, Virus recombinants.
- génétique : Sialidase, Virus recombinants.
- métabolisme : Sialidase.
- physiologie : Virus de la grippe A, Virus recombinants.
- virologie : Intestins.
- Amorces ADN, Animaux, Canards, Modèles moléculaires, Mutagenèse dirigée, Réplication virale, Sialidase, Substitution d'acide aminé, Séquence nucléotidique.

English descriptors

KwdEn :
- Amino Acid Substitution, Animals, Base Sequence, DNA Primers, Ducks, Influenza A virus (enzymology), Influenza A virus (growth & development), Influenza A virus (physiology), Intestines (virology), Models, Molecular, Mutagenesis, Site-Directed, Neuraminidase (chemistry), Neuraminidase (genetics), Neuraminidase (metabolism), Reassortant Viruses (enzymology), Reassortant Viruses (genetics), Reassortant Viruses (growth & development), Reassortant Viruses (physiology), Virus Replication.
MESH :
- chemical , chemistry : Neuraminidase.
- chemical , genetics : Neuraminidase.
- chemical , metabolism : Neuraminidase.
- chemical : DNA Primers.
- enzymology : Influenza A virus, Reassortant Viruses.
- genetics : Reassortant Viruses.
- growth & development : Influenza A virus, Reassortant Viruses.
- physiology : Influenza A virus, Reassortant Viruses.
- virology : Intestines.
- Amino Acid Substitution, Animals, Base Sequence, Ducks, Models, Molecular, Mutagenesis, Site-Directed, Virus Replication.

Abstract

The 1957 human pandemic strain of influenza A virus contained an avian virus hemagglutinin (HA) and neuraminidase (NA), both of which acquired specificity for the human receptor, N-acetylneuraminic acid linked to galactose of cellular glycoconjugates via an α2-6 bond (NeuAcα2-6Gal). Although the NA retained considerable specificity for NeuAcα2-3Gal, its original substrate in ducks, it lost the ability to support viral growth in the duck intestine, suggesting a growth-restrictive change other than a shift in substrate specificity. To test this possibility, we generated a panel of reassortant viruses that expressed the NA genes of human H2N2 viruses isolated from 1957 to 1968 with all other genes from the avian virus A/duck/Hong Kong/278/78 (H9N2). Only the NA of A/Singapore/1/57 supported efficient viral growth in the intestines of orally inoculated ducks. The growth-supporting capacity of the NA correlated with a high level of enzymatic activity, comparable to that found to be associated with avian virus NAs. The specific activities of the A/Ann Arbor/6/60 and A/England/12/62 NAs, which showed greatly restricted abilities to support viral growth in ducks, were only 8 and 5%, respectively, of the NA specific activity for A/Singapore/1/57. Using chimeric constructs based on A/Singapore/1/57 and A/England/12/62 NAs, we localized the determinants of high specific NA activity to a region containing six amino acid substitutions in A/England/12/62: Ser331→Arg, Asp339→Asn, Asn367→Ser, Ser370→Leu, Asn400→Ser, and Pro431→Glu. Five of these six residues (excluding Asn400) were required and sufficient for the full specific activity of the A/Singapore/1/57 NA. Thus, in addition to a change in substrate specificity, a reduction in high specific activity may be required for the adaptation of avian virus NAs to growth in humans. This change is likely needed to maintain an optimal balance between NA activity and the lower affinity shown by human virus HAs for their cellular receptor.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC114763

DOI: 10.1128/JVI.75.23.11773-11780.2001
PubMed: 11689658
PubMed Central: 114763

Affiliations:

Links to Exploration step

PMC:114763

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<term>Ducks</term>
<term>Influenza A virus (enzymology)</term>
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<term>Animaux</term>
<term>Canards</term>
<term>Intestins (virologie)</term>
<term>Modèles moléculaires</term>
<term>Mutagenèse dirigée</term>
<term>Réplication virale</term>
<term>Sialidase ()</term>
<term>Sialidase (génétique)</term>
<term>Sialidase (métabolisme)</term>
<term>Substitution d'acide aminé</term>
<term>Séquence nucléotidique</term>
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<term>Virus de la grippe A (enzymologie)</term>
<term>Virus de la grippe A (physiologie)</term>
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<term>Virus recombinants (enzymologie)</term>
<term>Virus recombinants (génétique)</term>
<term>Virus recombinants (physiologie)</term>
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<front><div type="abstract" xml:lang="en"><p>The 1957 human pandemic strain of influenza A virus contained an avian virus hemagglutinin (HA) and neuraminidase (NA), both of which acquired specificity for the human receptor, <italic>N</italic>
-acetylneuraminic acid linked to galactose of cellular glycoconjugates via an α2-6 bond (NeuAcα2-6Gal). Although the NA retained considerable specificity for NeuAcα2-3Gal, its original substrate in ducks, it lost the ability to support viral growth in the duck intestine, suggesting a growth-restrictive change other than a shift in substrate specificity. To test this possibility, we generated a panel of reassortant viruses that expressed the NA genes of human H2N2 viruses isolated from 1957 to 1968 with all other genes from the avian virus A/duck/Hong Kong/278/78 (H9N2). Only the NA of A/Singapore/1/57 supported efficient viral growth in the intestines of orally inoculated ducks. The growth-supporting capacity of the NA correlated with a high level of enzymatic activity, comparable to that found to be associated with avian virus NAs. The specific activities of the A/Ann Arbor/6/60 and A/England/12/62 NAs, which showed greatly restricted abilities to support viral growth in ducks, were only 8 and 5%, respectively, of the NA specific activity for A/Singapore/1/57. Using chimeric constructs based on A/Singapore/1/57 and A/England/12/62 NAs, we localized the determinants of high specific NA activity to a region containing six amino acid substitutions in A/England/12/62: Ser331→Arg, Asp339→Asn, Asn367→Ser, Ser370→Leu, Asn400→Ser, and Pro431→Glu. Five of these six residues (excluding Asn400) were required and sufficient for the full specific activity of the A/Singapore/1/57 NA. Thus, in addition to a change in substrate specificity, a reduction in high specific activity may be required for the adaptation of avian virus NAs to growth in humans. This change is likely needed to maintain an optimal balance between NA activity and the lower affinity shown by human virus HAs for their cellular receptor.</p>
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Amino Acids Responsible for the Absolute Sialidase Activity of the Influenza A Virus Neuraminidase: Relationship to Growth in the Duck Intestine

Amino Acids Responsible for the Absolute Sialidase Activity of the Influenza A Virus Neuraminidase: Relationship to Growth in the Duck Intestine

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

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