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 : 000352 ( PubMed/Corpus ); précédent : 000351; suivant : 000353Effect 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.
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
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pubmed:11961269Le document en format XML
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Hongo</name><affiliation><nlm:affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</nlm:affiliation></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></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></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></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></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:11961269</idno><idno type="pmid">11961269</idno><idno type="doi">10.1099/0022-1317-83-5-1137</idno><idno type="wicri:Area/PubMed/Corpus">000352</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000352</idno></publicationStmt><sourceDesc><biblStruct><analytic><title 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></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></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></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></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></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></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></affiliation></author></analytic><series><title level="j">The Journal of general virology</title><idno type="ISSN">0022-1317</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Monoclonal (immunology)</term><term>Biological Transport</term><term>COS Cells</term><term>Glycosylation</term><term>Hemagglutinin Glycoproteins, Influenza Virus (metabolism)</term><term>Mutagenesis, Site-Directed</term><term>Oligosaccharides (metabolism)</term><term>Rabbits</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" 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" 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></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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11961269</PMID><DateCompleted><Year>2002</Year><Month>06</Month><Day>12</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>19</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-1317</ISSN><JournalIssue CitedMedium="Print"><Volume>83</Volume><Issue>Pt 5</Issue><PubDate><Year>2002</Year><Month>May</Month></PubDate></JournalIssue><Title>The Journal of general virology</Title><ISOAbbreviation>J. Gen. Virol.</ISOAbbreviation></Journal><ArticleTitle>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.</ArticleTitle><Pagination><MedlinePgn>1137-1146</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1099/0022-1317-83-5-1137</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tsuchiya</LastName><ForeName>Emi</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sugawara</LastName><ForeName>Kanetsu</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hongo</LastName><ForeName>Seiji</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matsuzaki</LastName><ForeName>Yoko</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Muraki</LastName><ForeName>Yasushi</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Zhu-Nan</ForeName><Initials>ZN</Initials><AffiliationInfo><Affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>Kiyoto</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Bacteriology, Yamagata University School of Medicine, Iida-Nishi, Yamagata 990-9585, Japan1.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Gen Virol</MedlineTA><NlmUniqueID>0077340</NlmUniqueID><ISSNLinking>0022-1317</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019267">Hemagglutinin Glycoproteins, Influenza 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