Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses
Identifieur interne : 000101 ( 1957/Analysis ); précédent : 000100; suivant : 000102Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses
Auteurs : Jennifer Uhlendorff [Allemagne] ; Tatyana Matrosovich [Allemagne] ; Hans-Dieter Klenk [Allemagne] ; Mikhail Matrosovich [Allemagne]Source :
- Archives of Virology [ 0304-8608 ] ; 2009-06-01.
Descripteurs français
- KwdFr :
- Animaux, Chiens, Flambées de maladies, Grippe humaine (virologie), Grippe humaine (épidémiologie), Humains, Hémadsorption, Lignée cellulaire, Mutagenèse dirigée, Mutation faux-sens, Protéines virales (génétique), Protéines virales (métabolisme), Sialidase (génétique), Sialidase (métabolisme), Sites de fixation, Sous-type H1N1 du virus de la grippe A (génétique), Sous-type H2N2 du virus de la grippe A (génétique), Sous-type H2N2 du virus de la grippe A (pathogénicité), Substitution d'acide aminé (génétique).
- MESH :
- génétique : Protéines virales, Sialidase, Sous-type H1N1 du virus de la grippe A, Sous-type H2N2 du virus de la grippe A, Substitution d'acide aminé.
- métabolisme : Protéines virales, Sialidase.
- pathogénicité : Sous-type H2N2 du virus de la grippe A.
- virologie : Grippe humaine.
- épidémiologie : Grippe humaine.
- Animaux, Chiens, Flambées de maladies, Humains, Hémadsorption, Lignée cellulaire, Mutagenèse dirigée, Mutation faux-sens, Sites de fixation.
- Pascal (Inist)
English descriptors
- KwdEn :
- Amino Acid Substitution (genetics), Animals, Binding Sites, Cell Line, Chlorocebus aethiops, Disease Outbreaks, Dogs, Exo-α-sialidase, Hemadsorption, Humans, Influenza A Virus, H1N1 Subtype (genetics), Influenza A Virus, H2N2 Subtype (genetics), Influenza A Virus, H2N2 Subtype (pathogenicity), Influenza, Human (epidemiology), Influenza, Human (virology), Influenzavirus, Mutagenesis, Site-Directed, Mutation, Missense, Neuraminidase (genetics), Neuraminidase (metabolism), Viral Proteins (genetics), Viral Proteins (metabolism).
- MESH :
- chemical , genetics : Neuraminidase, Viral Proteins.
- epidemiology : Influenza, Human.
- genetics : Amino Acid Substitution, Influenza A Virus, H1N1 Subtype, Influenza A Virus, H2N2 Subtype.
- chemical , metabolism : Neuraminidase, Viral Proteins.
- pathogenicity : Influenza A Virus, H2N2 Subtype.
- virology : Influenza, Human.
- Animals, Binding Sites, Cell Line, Chlorocebus aethiops, Disease Outbreaks, Dogs, Hemadsorption, Humans, Mutagenesis, Site-Directed, Mutation, Missense.
Abstract
Abstract: Human influenza viruses derive their genes from avian viruses. The neuraminidase (NA) of the avian viruses has, in addition to the catalytic site, a separate sialic acid binding site (hemadsorption site) that is not present in human viruses. The biological significance of the NA hemadsorption activity in avian influenza viruses remained elusive. A sequence database analysis revealed that the NAs of the majority of human H2N2 viruses isolated during the influenza pandemic of 1957 differ from their putative avian precursor by amino acid substitutions in the hemadsorption site. We found that the NA of a representative pandemic virus A/Singapore/1/57 (H2N2) lacks hemadsorption activity and that a single reversion to the avian-virus-like sequence (N367S) restores hemadsorption. Using this hemadsorption-positive NA, we generated three NA variants with substitutions S370L, N400S and W403R that have been found in the hemadsorption site of human H2N2 viruses. Each substitution abolished hemadsorption activity. Although, there was no correlation between hemadsorption activity of the NA variants and their enzymatic activity with respect to monovalent substrates, all four hemadsorption-negative NAs desialylated macromolecular substrates significantly slower than did the hemadsorption-positive counterpart. The NA of the 1918 pandemic virus A/Brevig Mission/1/18 (H1N1) also differed from avian N1 NAs by reduced hemadsorption activity and less efficient hydrolysis of macromolecular substrates. Our data indicate that the hemadsorption site serves to enhance the catalytic efficiency of NA and they suggest that, in addition to changes in the receptor-binding specificity of the hemagglutinin, alterations of the NA are needed for the emergence of pandemic influenza viruses.
Url:
- https://api.istex.fr/ark:/67375/VQC-Q7CWW1GT-8/fulltext.pdf
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2691527
DOI: 10.1007/s00705-009-0393-x
Affiliations:
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ISTEX:D581EDCB9D9E9EE8B977AB9777561F2F7B853367Le document en format XML
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ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Human influenza viruses derive their genes from avian viruses. The neuraminidase (NA) of the avian viruses has, in addition to the catalytic site, a separate sialic acid binding site (hemadsorption site) that is not present in human viruses. The biological significance of the NA hemadsorption activity in avian influenza viruses remained elusive. A sequence database analysis revealed that the NAs of the majority of human H2N2 viruses isolated during the influenza pandemic of 1957 differ from their putative avian precursor by amino acid substitutions in the hemadsorption site. We found that the NA of a representative pandemic virus A/Singapore/1/57 (H2N2) lacks hemadsorption activity and that a single reversion to the avian-virus-like sequence (N367S) restores hemadsorption. Using this hemadsorption-positive NA, we generated three NA variants with substitutions S370L, N400S and W403R that have been found in the hemadsorption site of human H2N2 viruses. Each substitution abolished hemadsorption activity. Although, there was no correlation between hemadsorption activity of the NA variants and their enzymatic activity with respect to monovalent substrates, all four hemadsorption-negative NAs desialylated macromolecular substrates significantly slower than did the hemadsorption-positive counterpart. The NA of the 1918 pandemic virus A/Brevig Mission/1/18 (H1N1) also differed from avian N1 NAs by reduced hemadsorption activity and less efficient hydrolysis of macromolecular substrates. Our data indicate that the hemadsorption site serves to enhance the catalytic efficiency of NA and they suggest that, in addition to changes in the receptor-binding specificity of the hemagglutinin, alterations of the NA are needed for the emergence of pandemic influenza viruses.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country><region><li>District de Giessen</li><li>Hesse (Land)</li></region><settlement><li>Marbourg</li></settlement></list><tree><country name="Allemagne"><region name="Hesse (Land)"><name sortKey="Uhlendorff, Jennifer" sort="Uhlendorff, Jennifer" uniqKey="Uhlendorff J" first="Jennifer" last="Uhlendorff">Jennifer Uhlendorff</name></region><name sortKey="Klenk, Hans Dieter" sort="Klenk, Hans Dieter" uniqKey="Klenk H" first="Hans-Dieter" last="Klenk">Hans-Dieter Klenk</name><name sortKey="Matrosovich, Mikhail" sort="Matrosovich, Mikhail" uniqKey="Matrosovich M" first="Mikhail" last="Matrosovich">Mikhail Matrosovich</name><name sortKey="Matrosovich, Tatyana" sort="Matrosovich, Tatyana" uniqKey="Matrosovich T" first="Tatyana" last="Matrosovich">Tatyana Matrosovich</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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