Antigenic, sequence, and crystal variation in influenza B neuraminidase
Identifieur interne : 004A48 ( Main/Curation ); précédent : 004A47; suivant : 004A49Antigenic, sequence, and crystal variation in influenza B neuraminidase
Auteurs : Gillian M. Air [États-Unis] ; W. Graeme Laver [Australie] ; Ming Luo [États-Unis] ; Stephen J. Stray [États-Unis] ; Gayla Legrone [États-Unis] ; Robert G. Webster [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1990.
English descriptors
- Teeft :
- Academic press, Acid change, Amino, Amino acid, Amino acid sequence, Amino acid sequence changes, Amino acid sequences, Amino acids, Antibody, Antigenic, Antigenic drift, Antigenic properties, Antigenic variants, Cdna sequences, Cell membrane, Crystal morphology, Diffraction studies, Embryonated eggs, Enzyme activity, Field strains, Hemagglutinin, Hemagglutinin molecule, High variation, Hybridoma, Identical reactivities, Influenza, Influenza type, Influenza virus, Influenza virus neuraminidase, Influenza viruses, Laver, Monoclonal, Monoclonal antibodies, Mutant, Neuraminidase, Nucleotide, Nucleotide changes, Nucleotide sequence, Nucleotide sequences, Parental virus, Reassortant, Reassortant virus, Remarkable differences, Second reading frame, Sequence analysis, Sequence changes, Sequence conservation, Sequence variation, Structure determination, Surface glycoprotein, Vapor diffusion, Variable region, Viral, Virology, Virus, Virus neuraminidase.
Abstract
Abstract: The neuraminidase (NA) genes of influenza B viruses B/Maryland/59, B/Hong Kong/8/73, B/Singapore/222/79, B/Oregon/5/80, B/USSR/100/83, B/Victoria/3/85, B/Leningrad/179/86, B/Memphis/6/86, and B/Memphis/3/89 have been sequenced. The deduced amino acid sequences show high variability in the stalk domain of the NA, but a surprising degree of sequence conservation in the head region which carries all the antigenic and enzyme activity. The variable region coding for the neuraminidase stalk also translates into a variable section in the overlapping NB polypeptide, which is coded from a second reading frame that overlaps the first 100 amino acids of NA. The influenza B NAs are antigenically distinguishable with monoclonal antibodies in neuraminidase-inhibition tests, even when there is only one amino acid sequence difference. However, seven of nine escape mutants selected with monoclonal antibodies were distinguished only by the antibody used for selection. When NA heads of influenza B viruses are crystallized, there are remarkable differences in crystal morphology between neuraminidases which have very few sequence changes.
Url:
DOI: 10.1016/0042-6822(90)90523-T
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Box 318, Memphis, Tennessee 38101</wicri:regionArea><wicri:noRegion>Tennessee 38101</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="1990">1990</date><biblScope unit="volume">177</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="578">578</biblScope><biblScope unit="page" to="587">587</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>Academic press</term><term>Acid change</term><term>Amino</term><term>Amino acid</term><term>Amino acid sequence</term><term>Amino acid sequence changes</term><term>Amino acid sequences</term><term>Amino acids</term><term>Antibody</term><term>Antigenic</term><term>Antigenic drift</term><term>Antigenic properties</term><term>Antigenic variants</term><term>Cdna sequences</term><term>Cell membrane</term><term>Crystal morphology</term><term>Diffraction studies</term><term>Embryonated eggs</term><term>Enzyme activity</term><term>Field strains</term><term>Hemagglutinin</term><term>Hemagglutinin molecule</term><term>High variation</term><term>Hybridoma</term><term>Identical reactivities</term><term>Influenza</term><term>Influenza type</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Influenza viruses</term><term>Laver</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Mutant</term><term>Neuraminidase</term><term>Nucleotide</term><term>Nucleotide changes</term><term>Nucleotide sequence</term><term>Nucleotide sequences</term><term>Parental virus</term><term>Reassortant</term><term>Reassortant virus</term><term>Remarkable differences</term><term>Second reading frame</term><term>Sequence analysis</term><term>Sequence changes</term><term>Sequence conservation</term><term>Sequence variation</term><term>Structure determination</term><term>Surface glycoprotein</term><term>Vapor diffusion</term><term>Variable region</term><term>Viral</term><term>Virology</term><term>Virus</term><term>Virus neuraminidase</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The neuraminidase (NA) genes of influenza B viruses B/Maryland/59, B/Hong Kong/8/73, B/Singapore/222/79, B/Oregon/5/80, B/USSR/100/83, B/Victoria/3/85, B/Leningrad/179/86, B/Memphis/6/86, and B/Memphis/3/89 have been sequenced. The deduced amino acid sequences show high variability in the stalk domain of the NA, but a surprising degree of sequence conservation in the head region which carries all the antigenic and enzyme activity. The variable region coding for the neuraminidase stalk also translates into a variable section in the overlapping NB polypeptide, which is coded from a second reading frame that overlaps the first 100 amino acids of NA. The influenza B NAs are antigenically distinguishable with monoclonal antibodies in neuraminidase-inhibition tests, even when there is only one amino acid sequence difference. However, seven of nine escape mutants selected with monoclonal antibodies were distinguished only by the antibody used for selection. When NA heads of influenza B viruses are crystallized, there are remarkable differences in crystal morphology between neuraminidases which have very few sequence changes.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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