Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus.
Identifieur interne : 001807 ( Main/Exploration ); précédent : 001806; suivant : 001808Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus.
Auteurs : Emi Tsuchiya ; Kanetsu Sugawara ; Seiji Hongo ; Yoko Matsuzaki ; Yasushi Muraki ; Zhu-Nan Li ; Kiyoto NakamuraSource :
- The Journal of general virology [ 0022-1317 ] ; 2001.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , immunology : Antibodies, Monoclonal, Hemagglutinin Glycoproteins, Influenza Virus.
- immunology : Influenza A virus.
- Animals, Influenza A Virus, H2N2 Subtype, Mice, Mice, Inbred BALB C, Structure-Activity Relationship.
Abstract
The antigenic structure of influenza A/H2N2 virus haemagglutinin (HA) was analysed using 19 monoclonal antibodies (MAbs) against the HA of A/Kayano/57. The antibodies were classified into three groups: group I had both haemagglutination inhibition and neutralization activities, group II had neutralization activity but no haemagglutination inhibition activity and group III had neither activity. Analysis of escape mutants selected by each of the group I and II antibodies identified six distinct antigenic sites: four (I-A to I-D) were recognized by group I MAbs and two (II-A and II-B) were recognized by group II MAbs. Sequence analysis of the HA genes of the escape mutants demonstrated that sites I-A, I-B and I-C form a contiguous antigenic area that contains the regions corresponding to antigenic sites A, B and D on the H3 molecule and that sites I-D and II-B are the equivalents of sites E and C, respectively, suggesting that the antigenic structure of the H2 molecule is largely similar to that of the H3 molecule. However, the H2 molecule differed from the H3 molecule in having a highly conserved antigenic site (II-A) in the stem domain. It was also found that most of the escape mutants selected by antibodies to sites I-A, I-B and I-C acquired a new glycosylation site at position 160, 187 or 131, respectively, which indicates that A/H2N2 viruses have the potential to gain at least one additional oligosaccharide on the tip of the HA, although this has never occurred during 11 years of its circulation in humans.
DOI: 10.1099/0022-1317-82-10-2475
PubMed: 11562540
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 000357
- to stream PubMed, to step Curation: 000357
- to stream PubMed, to step Checkpoint: 000326
- to stream Ncbi, to step Merge: 000038
- to stream Ncbi, to step Curation: 000038
- to stream Ncbi, to step Checkpoint: 000038
- to stream Main, to step Merge: 001847
- to stream Main, to step Curation: 001807
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus.</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></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2001">2001</date><idno type="RBID">pubmed:11562540</idno><idno type="pmid">11562540</idno><idno type="doi">10.1099/0022-1317-82-10-2475</idno><idno type="wicri:Area/PubMed/Corpus">000357</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000357</idno><idno type="wicri:Area/PubMed/Curation">000357</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000357</idno><idno type="wicri:Area/PubMed/Checkpoint">000326</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000326</idno><idno type="wicri:Area/Ncbi/Merge">000038</idno><idno type="wicri:Area/Ncbi/Curation">000038</idno><idno type="wicri:Area/Ncbi/Checkpoint">000038</idno><idno type="wicri:doubleKey">0022-1317:2001:Tsuchiya E:antigenic:structure:of</idno><idno type="wicri:Area/Main/Merge">001847</idno><idno type="wicri:Area/Main/Curation">001807</idno><idno type="wicri:Area/Main/Exploration">001807</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus.</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="2001" type="published">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Monoclonal (immunology)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (chemistry)</term><term>Hemagglutinin Glycoproteins, Influenza Virus (immunology)</term><term>Influenza A Virus, H2N2 Subtype</term><term>Influenza A virus (immunology)</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Anticorps monoclonaux (immunologie)</term><term>Glycoprotéine hémagglutinine du virus influenza ()</term><term>Glycoprotéine hémagglutinine du virus influenza (immunologie)</term><term>Relation structure-activité</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Sous-type H2N2 du virus de la grippe A</term><term>Virus de la grippe A (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinin Glycoproteins, Influenza Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Influenza A Virus, H2N2 Subtype</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Relation structure-activité</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Sous-type H2N2 du virus de la grippe A</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The antigenic structure of influenza A/H2N2 virus haemagglutinin (HA) was analysed using 19 monoclonal antibodies (MAbs) against the HA of A/Kayano/57. The antibodies were classified into three groups: group I had both haemagglutination inhibition and neutralization activities, group II had neutralization activity but no haemagglutination inhibition activity and group III had neither activity. Analysis of escape mutants selected by each of the group I and II antibodies identified six distinct antigenic sites: four (I-A to I-D) were recognized by group I MAbs and two (II-A and II-B) were recognized by group II MAbs. Sequence analysis of the HA genes of the escape mutants demonstrated that sites I-A, I-B and I-C form a contiguous antigenic area that contains the regions corresponding to antigenic sites A, B and D on the H3 molecule and that sites I-D and II-B are the equivalents of sites E and C, respectively, suggesting that the antigenic structure of the H2 molecule is largely similar to that of the H3 molecule. However, the H2 molecule differed from the H3 molecule in having a highly conserved antigenic site (II-A) in the stem domain. It was also found that most of the escape mutants selected by antibodies to sites I-A, I-B and I-C acquired a new glycosylation site at position 160, 187 or 131, respectively, which indicates that A/H2N2 viruses have the potential to gain at least one additional oligosaccharide on the tip of the HA, although this has never occurred during 11 years of its circulation 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)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001807 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001807 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:11562540
|texte= Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:11562540" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a H2N2V1
| This area was generated with Dilib version V0.6.33. |  |