Influenza virus neuraminidase with hemagglutinin activity
Identifieur interne : 002511 ( Main/Exploration ); précédent : 002510; suivant : 002512Influenza virus neuraminidase with hemagglutinin activity
Auteurs : W. G. Laver [Australie] ; P. M. Colman [Australie] ; R. G. Webster [États-Unis] ; V. S. Hinshaw [États-Unis] ; G. M. Air [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1984.
English descriptors
- Teeft :
- Amino acid sequence, Ascitic fluid, Assay, Cell dimension, Cell receptors, Cellulose acetate strips, Different sites, Diffraction studies, Electron micrograph, Electron micrographs, Enzyme activity, Experiments show, Fetuin substrate, Form rosettes, Glycoprotein, Great barrier reef, Hemagglutinating, Hemagglutinating activities, Hemagglutinating neuraminidase, Hemagglutinin, Hemagglutinin activity, Hemagglutinin molecules, High levels, High titer, Hln9, Hyperimmune rabbit antiserum, Infectivity, Influenza, Influenza virus, Influenza virus neuraminidase, Influenza viruses, Inhibitor, Initial stages, Large rhombic dodecahedral crystals, Laver, Molecule, Monoclonal antibodies, Neuraminic acid, Neuraminidase, Neuraminidase activities, Neuraminidase heads, Neuraminidase molecules, Other hand, Paramyxovirus, Paramyxovirus glycoproteins, Pronase digestion, Receptor, Recombinant, Recombinant virus, Rosette, Same site, Scheid, Sendai virus, Separate sites, Sialic acid, Space group, Subtypes, Tern virus, Vapor diffusion, Virology, Virus, Virus particle, Virus particles.
Abstract
Abstract: Isolated intact influenza virus neuraminidase (NA) molecules of the N9 subtype have been found to possess hemagglutinin (HA) activity which, at equivalent protein concentration, was fourfold higher than that of isolated hemagglutinin molecules of the H3 subtype. The amino-terminal sequence of the N9 NA is the same as in neuraminidases of the eight other influenza A virus NA subtypes previously reported. Viruses possessing N9 NA therefore have two different HA activities and antibody to either HA or NA alone was incapable of inhibiting hemagglutination by the virus. However, antibody to the HA of an H1N9 virus neutralized its infectivity as effectively as it neutralized H1N1 or H1N2 viruses whose neuraminidases have no HA activity. (Antibodies to N9 NA did not neutralize the infectivity of viruses with N9 neuraminidase.) 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid inhibited N9 NA activity but had no effect on the HA activity of the isolated N9 NA. One interpretation of this result would be that the HA and NA activities are located in separate sites. Pronase-released N9 NA heads form crystals suitable for X-ray diffraction studies and preliminary data to 2.9 Å establish the space group as cubic, I432 with cell dimension a = 184 A ̊. Data extend to beyond 1.9 Å resolution, and these will be collected in the future.
Url:
DOI: 10.1016/0042-6822(84)90223-X
Affiliations:
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G." last="Laver">W. G. Laver</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>John Curtin School of Medical Research, Australian National University, Canberra ACT 2601</wicri:regionArea><wicri:noRegion>Canberra ACT 2601</wicri:noRegion></affiliation></author><author><name sortKey="Colman, P M" sort="Colman, P M" uniqKey="Colman P" first="P. M." last="Colman">P. M. Colman</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>CSIRO, Division of Protein Chemistry, 343 Royal Parade, Parkville, Victoria 3052</wicri:regionArea><wicri:noRegion>Victoria 3052</wicri:noRegion></affiliation></author><author><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R. G." last="Webster">R. G. Webster</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, P.O. Box 318, Memphis, Tennessee 38101</wicri:regionArea><wicri:noRegion>Tennessee 38101</wicri:noRegion></affiliation></author><author><name sortKey="Hinshaw, V S" sort="Hinshaw, V S" uniqKey="Hinshaw V" first="V. S." last="Hinshaw">V. S. Hinshaw</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, P.O. Box 318, Memphis, Tennessee 38101</wicri:regionArea><wicri:noRegion>Tennessee 38101</wicri:noRegion></affiliation></author><author><name sortKey="Air, G M" sort="Air, G M" uniqKey="Air G" first="G. M." last="Air">G. M. Air</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology, University of Alabama, Birmingham, Alabama 35294</wicri:regionArea><wicri:noRegion>Alabama 35294</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1984">1984</date><biblScope unit="volume">137</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="314">314</biblScope><biblScope unit="page" to="323">323</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino acid sequence</term><term>Ascitic fluid</term><term>Assay</term><term>Cell dimension</term><term>Cell receptors</term><term>Cellulose acetate strips</term><term>Different sites</term><term>Diffraction studies</term><term>Electron micrograph</term><term>Electron micrographs</term><term>Enzyme activity</term><term>Experiments show</term><term>Fetuin substrate</term><term>Form rosettes</term><term>Glycoprotein</term><term>Great barrier reef</term><term>Hemagglutinating</term><term>Hemagglutinating activities</term><term>Hemagglutinating neuraminidase</term><term>Hemagglutinin</term><term>Hemagglutinin activity</term><term>Hemagglutinin molecules</term><term>High levels</term><term>High titer</term><term>Hln9</term><term>Hyperimmune rabbit antiserum</term><term>Infectivity</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Influenza viruses</term><term>Inhibitor</term><term>Initial stages</term><term>Large rhombic dodecahedral crystals</term><term>Laver</term><term>Molecule</term><term>Monoclonal antibodies</term><term>Neuraminic acid</term><term>Neuraminidase</term><term>Neuraminidase activities</term><term>Neuraminidase heads</term><term>Neuraminidase molecules</term><term>Other hand</term><term>Paramyxovirus</term><term>Paramyxovirus glycoproteins</term><term>Pronase digestion</term><term>Receptor</term><term>Recombinant</term><term>Recombinant virus</term><term>Rosette</term><term>Same site</term><term>Scheid</term><term>Sendai virus</term><term>Separate sites</term><term>Sialic acid</term><term>Space group</term><term>Subtypes</term><term>Tern virus</term><term>Vapor diffusion</term><term>Virology</term><term>Virus</term><term>Virus particle</term><term>Virus particles</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Isolated intact influenza virus neuraminidase (NA) molecules of the N9 subtype have been found to possess hemagglutinin (HA) activity which, at equivalent protein concentration, was fourfold higher than that of isolated hemagglutinin molecules of the H3 subtype. The amino-terminal sequence of the N9 NA is the same as in neuraminidases of the eight other influenza A virus NA subtypes previously reported. Viruses possessing N9 NA therefore have two different HA activities and antibody to either HA or NA alone was incapable of inhibiting hemagglutination by the virus. However, antibody to the HA of an H1N9 virus neutralized its infectivity as effectively as it neutralized H1N1 or H1N2 viruses whose neuraminidases have no HA activity. (Antibodies to N9 NA did not neutralize the infectivity of viruses with N9 neuraminidase.) 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid inhibited N9 NA activity but had no effect on the HA activity of the isolated N9 NA. One interpretation of this result would be that the HA and NA activities are located in separate sites. Pronase-released N9 NA heads form crystals suitable for X-ray diffraction studies and preliminary data to 2.9 Å establish the space group as cubic, I432 with cell dimension a = 184 A ̊. Data extend to beyond 1.9 Å resolution, and these will be collected in the future.</div></front></TEI><affiliations><list><country><li>Australie</li><li>États-Unis</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W. G." last="Laver">W. G. Laver</name></noRegion><name sortKey="Colman, P M" sort="Colman, P M" uniqKey="Colman P" first="P. M." last="Colman">P. M. Colman</name></country><country name="États-Unis"><noRegion><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R. G." last="Webster">R. G. Webster</name></noRegion><name sortKey="Air, G M" sort="Air, G M" uniqKey="Air G" first="G. M." last="Air">G. M. Air</name><name sortKey="Hinshaw, V S" sort="Hinshaw, V S" uniqKey="Hinshaw V" first="V. S." last="Hinshaw">V. S. Hinshaw</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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