Effect of addition of new oligosaccharide chains to the globular head of influenza A/H2N2 virus haemagglutinin on the intracellular transport and biological activities of the molecule.
Identifieur interne : 001750 ( Main/Exploration ); précédent : 001749; suivant : 001751Effect of addition of new oligosaccharide chains to the globular head of influenza A/H2N2 virus haemagglutinin on the intracellular transport and biological activities of the molecule.
Auteurs : Emi Tsuchiya ; Kanetsu Sugawara ; Seiji Hongo ; Yoko Matsuzaki ; Yasushi Muraki ; Zhu-Nan Li ; Kiyoto NakamuraSource :
- The Journal of general virology [ 0022-1317 ] ; 2002.
Descripteurs français
- KwdFr :
- MESH :
- immunologie : Anticorps monoclonaux.
- métabolisme : Glycoprotéine hémagglutinine du virus influenza, Oligosaccharides.
- Animaux, Cellules COS, Glycosylation, Lapins, Mutagenèse dirigée, Relation structure-activité, Transport biologique.
English descriptors
- KwdEn :
- MESH :
- chemical , immunology : Antibodies, Monoclonal.
- chemical , metabolism : Hemagglutinin Glycoproteins, Influenza Virus, Oligosaccharides.
- Animals, Biological Transport, COS Cells, Glycosylation, Mutagenesis, Site-Directed, Rabbits, Structure-Activity Relationship.
Abstract
The haemagglutinin (HA) of influenza A/H2N2 virus possesses six antigenic sites (I-A to I-D, II-A and II-B), and sites I-A, I-B and I-C are located in the regions corresponding to sites A, B and D on the H3 HA. We demonstrated previously that most escape mutants selected by mAbs to site I-A, I-B or I-C had acquired a new oligosaccharide at position 160, 187 or 131, respectively, but this has never occurred during circulation of A/H2N2 virus in humans. Here, to examine whether the H2 HA has the potential to gain two new oligosaccharides on its tip, 31 double escape mutants were isolated by using a single escape mutant with an oligosaccharide at position 160, 187 or 131 as a parental virus and a mAb to an antigenic site different from that to which the mAb used for selection of the parental virus was directed as a selecting antibody, but there were no mutants with two new oligosaccharides. Glycosylation-site HA mutants containing one to three oligosaccharides at positions 160, 187 and 131 were also constructed and their intracellular transport and biological activities were analysed. The results showed that all of the mutant HAs were transported to the cell surface but exhibited a decrease in both receptor-binding and cell-fusing activities. Thus, influenza A/H2N2 virus may have failed to increase the number of oligosaccharides on the HA because, if this happens, the biological activities of the HA are reduced, decreasing the ability of the virus to replicate in humans.
DOI: 10.1099/0022-1317-83-5-1137
PubMed: 11961269
Affiliations:
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Le document en format XML
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xml:lang="en">Effect of addition of new oligosaccharide chains to the globular head of influenza A/H2N2 virus haemagglutinin on the intracellular transport and biological activities of the molecule.</title><author><name sortKey="Tsuchiya, Emi" sort="Tsuchiya, Emi" uniqKey="Tsuchiya E" first="Emi" last="Tsuchiya">Emi Tsuchiya</name><affiliation><nlm:affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</nlm:affiliation><wicri:noCountry code="subField">Japan1</wicri:noCountry></affiliation></author><author><name sortKey="Sugawara, Kanetsu" sort="Sugawara, Kanetsu" uniqKey="Sugawara K" first="Kanetsu" last="Sugawara">Kanetsu Sugawara</name><affiliation><nlm:affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</nlm:affiliation><wicri:noCountry code="subField">Japan1</wicri:noCountry></affiliation></author><author><name sortKey="Hongo, Seiji" sort="Hongo, Seiji" uniqKey="Hongo S" first="Seiji" last="Hongo">Seiji Hongo</name><affiliation><nlm:affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</nlm:affiliation><wicri:noCountry code="subField">Japan1</wicri:noCountry></affiliation></author><author><name sortKey="Matsuzaki, Yoko" sort="Matsuzaki, Yoko" uniqKey="Matsuzaki Y" first="Yoko" last="Matsuzaki">Yoko Matsuzaki</name><affiliation><nlm:affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</nlm:affiliation><wicri:noCountry code="subField">Japan1</wicri:noCountry></affiliation></author><author><name sortKey="Muraki, Yasushi" sort="Muraki, Yasushi" uniqKey="Muraki Y" first="Yasushi" last="Muraki">Yasushi Muraki</name><affiliation><nlm:affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</nlm:affiliation><wicri:noCountry code="subField">Japan1</wicri:noCountry></affiliation></author><author><name sortKey="Li, Zhu Nan" sort="Li, Zhu Nan" uniqKey="Li Z" first="Zhu-Nan" last="Li">Zhu-Nan Li</name><affiliation><nlm:affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</nlm:affiliation><wicri:noCountry code="subField">Japan1</wicri:noCountry></affiliation></author><author><name sortKey="Nakamura, Kiyoto" sort="Nakamura, Kiyoto" uniqKey="Nakamura K" first="Kiyoto" last="Nakamura">Kiyoto Nakamura</name><affiliation><nlm:affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</nlm:affiliation><wicri:noCountry code="subField">Japan1</wicri:noCountry></affiliation></author></analytic><series><title level="j">The Journal of general virology</title><idno type="ISSN">0022-1317</idno><imprint><date when="2002" 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xml:lang="en"><term>Antibodies, Monoclonal</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Oligosaccharides</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Oligosaccharides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Biological Transport</term><term>COS Cells</term><term>Glycosylation</term><term>Mutagenesis, Site-Directed</term><term>Rabbits</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules COS</term><term>Glycosylation</term><term>Lapins</term><term>Mutagenèse dirigée</term><term>Relation structure-activité</term><term>Transport biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The haemagglutinin (HA) of influenza A/H2N2 virus possesses six antigenic sites (I-A to I-D, II-A and II-B), and sites I-A, I-B and I-C are located in the regions corresponding to sites A, B and D on the H3 HA. We demonstrated previously that most escape mutants selected by mAbs to site I-A, I-B or I-C had acquired a new oligosaccharide at position 160, 187 or 131, respectively, but this has never occurred during circulation of A/H2N2 virus in humans. Here, to examine whether the H2 HA has the potential to gain two new oligosaccharides on its tip, 31 double escape mutants were isolated by using a single escape mutant with an oligosaccharide at position 160, 187 or 131 as a parental virus and a mAb to an antigenic site different from that to which the mAb used for selection of the parental virus was directed as a selecting antibody, but there were no mutants with two new oligosaccharides. Glycosylation-site HA mutants containing one to three oligosaccharides at positions 160, 187 and 131 were also constructed and their intracellular transport and biological activities were analysed. The results showed that all of the mutant HAs were transported to the cell surface but exhibited a decrease in both receptor-binding and cell-fusing activities. Thus, influenza A/H2N2 virus may have failed to increase the number of oligosaccharides on the HA because, if this happens, the biological activities of the HA are reduced, decreasing the ability of the virus to replicate in humans.</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="Li, Zhu Nan" sort="Li, Zhu Nan" uniqKey="Li Z" first="Zhu-Nan" last="Li">Zhu-Nan Li</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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