Identification of amino acids in H9N2 influenza virus neuraminidase that are critical for the binding of two mouse monoclonal antibodies.
Identifieur interne : 000537 ( PubMed/Curation ); précédent : 000536; suivant : 000538Identification of amino acids in H9N2 influenza virus neuraminidase that are critical for the binding of two mouse monoclonal antibodies.
Auteurs : Zhimin Wan [République populaire de Chine] ; Jianqiang Ye [République populaire de Chine] ; Jianjun Sang [République populaire de Chine] ; Hongxia Shao [République populaire de Chine] ; Kun Qian [République populaire de Chine] ; Wenjie Jin [République populaire de Chine] ; Aijian Qin [République populaire de Chine] ; Hongquan Wan [République populaire de Chine]Source :
- Veterinary microbiology [ 1873-2542 ] ; 2016.
Descripteurs français
- KwdFr :
- Acides aminés (), Acides aminés (métabolisme), Animaux, Anticorps antiviraux (métabolisme), Anticorps monoclonaux (métabolisme), Liaison aux protéines (génétique), Modèles moléculaires, Mutation, Sialidase (), Sialidase (génétique), Souris, Sous-type H9N2 du virus de la grippe A (génétique), Structure tertiaire des protéines, Séquence d'acides aminés, Épitopes (métabolisme).
- MESH :
- génétique : Liaison aux protéines, Sialidase, Sous-type H9N2 du virus de la grippe A.
- métabolisme : Acides aminés, Anticorps antiviraux, Anticorps monoclonaux, Épitopes.
- Acides aminés, Animaux, Modèles moléculaires, Mutation, Sialidase, Souris, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acids (chemistry), Amino Acids (metabolism), Animals, Antibodies, Monoclonal (metabolism), Antibodies, Viral (metabolism), Epitopes (metabolism), Influenza A Virus, H9N2 Subtype (genetics), Mice, Models, Molecular, Mutation, Neuraminidase (chemistry), Neuraminidase (genetics), Protein Binding (genetics), Protein Structure, Tertiary.
- MESH :
- chemical , chemistry : Amino Acids, Neuraminidase.
- chemical , genetics : Neuraminidase.
- chemical , metabolism : Amino Acids, Antibodies, Monoclonal, Antibodies, Viral, Epitopes.
- genetics : Influenza A Virus, H9N2 Subtype, Protein Binding.
- Amino Acid Sequence, Animals, Mice, Models, Molecular, Mutation, Protein Structure, Tertiary.
Abstract
Neuraminidase (NA) is one of the major glycoproteins on the surface of influenza virus. It cleaves the linkage between haemagglutinin and cell surface receptors, and thus helps the release and spread of influenza virus. Despite the importance of H9N2 virus in influenza pandemic preparedness, the antigenic characteristics of its surface glycoproteins, especially NA, remains to be investigated. In the present study, we characterized two monoclonal antibodies (mAbs), 1D1 and 1G8, which are against the NA of an H9N2 virus A/Chicken/Jiangsu/X1/2004 (X1). We examined the inhibitory effect of these mAbs in two NA inhibition assays: enzyme-linked lectin assay (ELLA) and 2'-(4-methylumbelliferyl)-a-d-N-acetylneuraminic acid (Mu-NANA) assay. In ELLA, which uses a large molecule fetuin (molecular weight: 50kd) as substrate, both antibodies effectively inhibit the NA activity of X1 virus. However, in Mu-NANA assay, which uses the small molecule Mu-NANA (molecular weight: 489 d) as substrate, antibody 1G8 inhibits the NA activity, while antibody 1D1 does not. Three amino acid mutations, at positions 198, 199 and 338, respectively, were detected in the NA of escape mutants of X1 virus selected with the two antibodies. Natural mutations at these three positions have occurred, indicative of immune pressure on H9N2 virus in the field. Our findings lay a basis for detailed investigation on the antigenic structure of H9N2 virus NA, which may be helpful for developing NA-based antibody reagents as well as vaccines.
DOI: 10.1016/j.vetmic.2016.03.011
PubMed: 27066709
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Electronic address: aijian@yzu.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009</wicri:regionArea></affiliation></author><author><name sortKey="Wan, Hongquan" sort="Wan, Hongquan" uniqKey="Wan H" first="Hongquan" last="Wan">Hongquan Wan</name><affiliation wicri:level="1"><nlm:affiliation>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009, China. Electronic address: hqwan129@yahoo.com.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009</wicri:regionArea></affiliation></author></analytic><series><title level="j">Veterinary microbiology</title><idno type="eISSN">1873-2542</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acids (chemistry)</term><term>Amino Acids (metabolism)</term><term>Animals</term><term>Antibodies, Monoclonal (metabolism)</term><term>Antibodies, Viral (metabolism)</term><term>Epitopes (metabolism)</term><term>Influenza A Virus, H9N2 Subtype (genetics)</term><term>Mice</term><term>Models, Molecular</term><term>Mutation</term><term>Neuraminidase (chemistry)</term><term>Neuraminidase (genetics)</term><term>Protein Binding (genetics)</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés ()</term><term>Acides aminés (métabolisme)</term><term>Animaux</term><term>Anticorps antiviraux (métabolisme)</term><term>Anticorps monoclonaux (métabolisme)</term><term>Liaison aux protéines (génétique)</term><term>Modèles moléculaires</term><term>Mutation</term><term>Sialidase ()</term><term>Sialidase (génétique)</term><term>Souris</term><term>Sous-type H9N2 du virus de la grippe A (génétique)</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Épitopes (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acids</term><term>Antibodies, Monoclonal</term><term>Antibodies, Viral</term><term>Epitopes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Influenza A Virus, H9N2 Subtype</term><term>Protein Binding</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Liaison aux protéines</term><term>Sialidase</term><term>Sous-type H9N2 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides aminés</term><term>Anticorps antiviraux</term><term>Anticorps monoclonaux</term><term>Épitopes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Mice</term><term>Models, Molecular</term><term>Mutation</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acides aminés</term><term>Animaux</term><term>Modèles moléculaires</term><term>Mutation</term><term>Sialidase</term><term>Souris</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Neuraminidase (NA) is one of the major glycoproteins on the surface of influenza virus. It cleaves the linkage between haemagglutinin and cell surface receptors, and thus helps the release and spread of influenza virus. Despite the importance of H9N2 virus in influenza pandemic preparedness, the antigenic characteristics of its surface glycoproteins, especially NA, remains to be investigated. In the present study, we characterized two monoclonal antibodies (mAbs), 1D1 and 1G8, which are against the NA of an H9N2 virus A/Chicken/Jiangsu/X1/2004 (X1). We examined the inhibitory effect of these mAbs in two NA inhibition assays: enzyme-linked lectin assay (ELLA) and 2'-(4-methylumbelliferyl)-a-d-N-acetylneuraminic acid (Mu-NANA) assay. In ELLA, which uses a large molecule fetuin (molecular weight: 50kd) as substrate, both antibodies effectively inhibit the NA activity of X1 virus. However, in Mu-NANA assay, which uses the small molecule Mu-NANA (molecular weight: 489 d) as substrate, antibody 1G8 inhibits the NA activity, while antibody 1D1 does not. Three amino acid mutations, at positions 198, 199 and 338, respectively, were detected in the NA of escape mutants of X1 virus selected with the two antibodies. Natural mutations at these three positions have occurred, indicative of immune pressure on H9N2 virus in the field. Our findings lay a basis for detailed investigation on the antigenic structure of H9N2 virus NA, which may be helpful for developing NA-based antibody reagents as well as vaccines. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27066709</PMID><DateCompleted><Year>2016</Year><Month>10</Month><Day>13</Day></DateCompleted><DateRevised><Year>2017</Year><Month>08</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-2542</ISSN><JournalIssue CitedMedium="Internet"><Volume>187</Volume><PubDate><Year>2016</Year><Month>May</Month><Day>01</Day></PubDate></JournalIssue><Title>Veterinary microbiology</Title><ISOAbbreviation>Vet. Microbiol.</ISOAbbreviation></Journal><ArticleTitle>Identification of amino acids in H9N2 influenza virus neuraminidase that are critical for the binding of two mouse monoclonal antibodies.</ArticleTitle><Pagination><MedlinePgn>58-63</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0378-1135(16)30064-5</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.vetmic.2016.03.011</ELocationID><Abstract><AbstractText>Neuraminidase (NA) is one of the major glycoproteins on the surface of influenza virus. It cleaves the linkage between haemagglutinin and cell surface receptors, and thus helps the release and spread of influenza virus. Despite the importance of H9N2 virus in influenza pandemic preparedness, the antigenic characteristics of its surface glycoproteins, especially NA, remains to be investigated. In the present study, we characterized two monoclonal antibodies (mAbs), 1D1 and 1G8, which are against the NA of an H9N2 virus A/Chicken/Jiangsu/X1/2004 (X1). We examined the inhibitory effect of these mAbs in two NA inhibition assays: enzyme-linked lectin assay (ELLA) and 2'-(4-methylumbelliferyl)-a-d-N-acetylneuraminic acid (Mu-NANA) assay. In ELLA, which uses a large molecule fetuin (molecular weight: 50kd) as substrate, both antibodies effectively inhibit the NA activity of X1 virus. However, in Mu-NANA assay, which uses the small molecule Mu-NANA (molecular weight: 489 d) as substrate, antibody 1G8 inhibits the NA activity, while antibody 1D1 does not. Three amino acid mutations, at positions 198, 199 and 338, respectively, were detected in the NA of escape mutants of X1 virus selected with the two antibodies. Natural mutations at these three positions have occurred, indicative of immune pressure on H9N2 virus in the field. Our findings lay a basis for detailed investigation on the antigenic structure of H9N2 virus NA, which may be helpful for developing NA-based antibody reagents as well as vaccines. </AbstractText><CopyrightInformation>Copyright © 2016 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wan</LastName><ForeName>Zhimin</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ye</LastName><ForeName>Jianqiang</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sang</LastName><ForeName>Jianjun</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shao</LastName><ForeName>Hongxia</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Qian</LastName><ForeName>Kun</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jin</LastName><ForeName>Wenjie</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Qin</LastName><ForeName>Aijian</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009, China. Electronic address: aijian@yzu.edu.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wan</LastName><ForeName>Hongquan</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>College of Veterinary Medicine, Yangzhou University, Yangzhou, 225009, China. Electronic address: hqwan129@yahoo.com.</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><ArticleDate DateType="Electronic"><Year>2016</Year><Month>03</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Vet Microbiol</MedlineTA><NlmUniqueID>7705469</NlmUniqueID><ISSNLinking>0378-1135</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000914">Antibodies, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000939">Epitopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.18</RegistryNumber><NameOfSubstance UI="D009439">Neuraminidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000914" MajorTopicYN="N">Antibodies, Viral</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000939" MajorTopicYN="N">Epitopes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053127" MajorTopicYN="N">Influenza A Virus, H9N2 Subtype</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009439" MajorTopicYN="N">Neuraminidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Amino acid</Keyword><Keyword MajorTopicYN="N">Escape mutant</Keyword><Keyword MajorTopicYN="N">H9N2 virus</Keyword><Keyword MajorTopicYN="N">Neuraminidase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>10</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>03</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>03</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>4</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>4</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>10</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27066709</ArticleId><ArticleId IdType="pii">S0378-1135(16)30064-5</ArticleId><ArticleId IdType="doi">10.1016/j.vetmic.2016.03.011</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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