Role of overlapping glycosylation sequons in antigenic properties, intracellular transport and biological activities of influenza A/H2N2 virus haemagglutinin.
Identifieur interne : 001744 ( Main/Exploration ); précédent : 001743; suivant : 001745Role of overlapping glycosylation sequons in antigenic properties, intracellular transport and biological activities of influenza A/H2N2 virus haemagglutinin.
Auteurs : Emi Tsuchiya ; Kanetsu Sugawara ; Seiji Hongo ; Yoko Matsuzaki ; Yasushi Muraki ; Kiyoto NakamuraSource :
- The Journal of general virology [ 0022-1317 ] ; 2002.
Descripteurs français
- KwdFr :
- Animaux, Anticorps monoclonaux (immunologie), Cellules COS, Fusion cellulaire, Glycoprotéine hémagglutinine du virus influenza (), Glycoprotéine hémagglutinine du virus influenza (génétique), Glycoprotéine hémagglutinine du virus influenza (immunologie), Glycoprotéine hémagglutinine du virus influenza (métabolisme), Glycosylation, Humains, Hémadsorption, Oligosaccharides, Relation structure-activité, Sous-type H2N2 du virus de la grippe A, Transport biologique, Virus de la grippe A (), Virus de la grippe A (immunologie), Virus de la grippe A (métabolisme).
- MESH :
- génétique : Glycoprotéine hémagglutinine du virus influenza.
- immunologie : Anticorps monoclonaux, Glycoprotéine hémagglutinine du virus influenza, Virus de la grippe A.
- métabolisme : Glycoprotéine hémagglutinine du virus influenza, Virus de la grippe A.
- Animaux, Cellules COS, Fusion cellulaire, Glycoprotéine hémagglutinine du virus influenza, Glycosylation, Humains, Hémadsorption, Oligosaccharides, Relation structure-activité, Sous-type H2N2 du virus de la grippe A, Transport biologique, Virus de la grippe A.
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (immunology), Biological Transport, COS Cells, Cell Fusion, Glycosylation, Hemadsorption, Hemagglutinin Glycoproteins, Influenza Virus (chemistry), Hemagglutinin Glycoproteins, Influenza Virus (genetics), Hemagglutinin Glycoproteins, Influenza Virus (immunology), Hemagglutinin Glycoproteins, Influenza Virus (metabolism), Humans, Influenza A Virus, H2N2 Subtype, Influenza A virus (chemistry), Influenza A virus (immunology), Influenza A virus (metabolism), Oligosaccharides, Structure-Activity Relationship.
- MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , genetics : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , immunology : Antibodies, Monoclonal, Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus.
- chemistry : Influenza A virus.
- immunology : Influenza A virus.
- metabolism : Influenza A virus.
- Animals, Biological Transport, COS Cells, Cell Fusion, Glycosylation, Hemadsorption, Humans, Influenza A Virus, H2N2 Subtype, Oligosaccharides, Structure-Activity Relationship.
Abstract
The haemagglutinin (HA) protein of influenza A/H2N2 virus possesses five oligosaccharide attachment sites, two of which have overlapping glycosylation sequons at positions 20-23 (NNST) and 169-172 (NNTS). Here, the role of these two oligosaccharide attachment sites is investigated with regard to antigenic property, intracellular transport and biological activity of the HA protein. Glycosylation-site HA mutants with mutation(s) in their overlapping glycosylated sequons, each of which had one or two oligosaccharide attachment sites removed, were constructed. Comparison of electrophoretic mobility between the wt and mutant HA proteins showed that both Asn residues 20 and 21 and Asn residues 169 and 170 could be used for glycosylation. Analysis of reactivity of the mutants with anti-HA monoclonal antibodies suggested that amino acid changes at these two positions result in a conformational change of the HA molecule. Even if oligosaccharide chains linked to Asn 20 or 21 and Asn 169 or 170 are eliminated, the antigenic properties, intracellular transport and biological activities are not influenced strongly. Thus it is reasonable to conclude that the two overlapping glycosylation sequons at positions 20-23 and 169-172 are conserved among all of the HAs of influenza A/H2N2 viruses because conservation of the amino acid sequence itself rather than that of N-glycosylation is essential for the formation of the proper conformation, intracellular transport and biological activities of the H2 subtype HA.
DOI: 10.1099/0022-1317-83-12-3067
PubMed: 12466483
Affiliations:
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Le document en format XML
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structure-activité</term><term>Sous-type H2N2 du virus de la grippe A</term><term>Transport biologique</term><term>Virus de la grippe A</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The haemagglutinin (HA) protein of influenza A/H2N2 virus possesses five oligosaccharide attachment sites, two of which have overlapping glycosylation sequons at positions 20-23 (NNST) and 169-172 (NNTS). Here, the role of these two oligosaccharide attachment sites is investigated with regard to antigenic property, intracellular transport and biological activity of the HA protein. Glycosylation-site HA mutants with mutation(s) in their overlapping glycosylated sequons, each of which had one or two oligosaccharide attachment sites removed, were constructed. Comparison of electrophoretic mobility between the wt and mutant HA proteins showed that both Asn residues 20 and 21 and Asn residues 169 and 170 could be used for glycosylation. Analysis of reactivity of the mutants with anti-HA monoclonal antibodies suggested that amino acid changes at these two positions result in a conformational change of the HA molecule. Even if oligosaccharide chains linked to Asn 20 or 21 and Asn 169 or 170 are eliminated, the antigenic properties, intracellular transport and biological activities are not influenced strongly. Thus it is reasonable to conclude that the two overlapping glycosylation sequons at positions 20-23 and 169-172 are conserved among all of the HAs of influenza A/H2N2 viruses because conservation of the amino acid sequence itself rather than that of N-glycosylation is essential for the formation of the proper conformation, intracellular transport and biological activities of the H2 subtype HA.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Hongo, Seiji" sort="Hongo, Seiji" uniqKey="Hongo S" first="Seiji" last="Hongo">Seiji Hongo</name><name sortKey="Matsuzaki, Yoko" sort="Matsuzaki, Yoko" uniqKey="Matsuzaki Y" first="Yoko" last="Matsuzaki">Yoko Matsuzaki</name><name sortKey="Muraki, Yasushi" sort="Muraki, Yasushi" uniqKey="Muraki Y" first="Yasushi" last="Muraki">Yasushi Muraki</name><name sortKey="Nakamura, Kiyoto" sort="Nakamura, Kiyoto" uniqKey="Nakamura K" first="Kiyoto" last="Nakamura">Kiyoto Nakamura</name><name sortKey="Sugawara, Kanetsu" sort="Sugawara, Kanetsu" uniqKey="Sugawara K" first="Kanetsu" last="Sugawara">Kanetsu Sugawara</name><name sortKey="Tsuchiya, Emi" sort="Tsuchiya, Emi" uniqKey="Tsuchiya E" first="Emi" last="Tsuchiya">Emi Tsuchiya</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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