Preparation-conditioned changes of the antigenicity of influenza virus neuraminidases.
Identifieur interne : 000636 ( PubMed/Corpus ); précédent : 000635; suivant : 000637Preparation-conditioned changes of the antigenicity of influenza virus neuraminidases.
Auteurs : U. DesselbergerSource :
- Archives of virology [ 0304-8608 ] ; 1977.
English descriptors
- KwdEn :
- Animals, Antibodies, Viral (biosynthesis), Antigens, Viral (analysis), Bromelains (pharmacology), Chick Embryo, Culture Techniques, Edetic Acid (pharmacology), Epitopes, Guinea Pigs, Hemagglutinins, Viral (analysis), Influenza A virus (analysis), Influenza A virus (drug effects), Influenza A virus (immunology), Mercaptoethanol (pharmacology), Neuraminidase (immunology), Nitrogen (analysis), Recombination, Genetic, Vaccination.
- MESH :
- chemical , analysis : Antigens, Viral, Hemagglutinins, Viral, Nitrogen.
- chemical , biosynthesis : Antibodies, Viral.
- chemical , immunology : Neuraminidase.
- chemical , pharmacology : Bromelains, Edetic Acid, Mercaptoethanol.
- analysis : Influenza A virus.
- drug effects : Influenza A virus.
- immunology : Influenza A virus.
- Animals, Chick Embryo, Culture Techniques, Epitopes, Guinea Pigs, Recombination, Genetic, Vaccination.
Abstract
The influenza virus strains A/Sing/1/57 (H2N2), A/Bel/42 (H0N1) and A/Bel/42 (HO)-A/Sing/1/57 (N2) were treated with bromelain under reducing conditions and with reducing agent alone, and the antigenicity of the neuraminidase (NA) of intact virus and of the split products was tested comparatively. It was found that the antigenicity of NA was influenced quantitatively and qualitatively by the preparation procedure. Antineuraminidase (AN) antibodies obtained after vaccination of guinea pigs with intact virus and with split products differed in their cross-reactivity with heterologous neuraminidases. In several cases, the quantity of AN antibody formation depended on the hemagglutinin (HA) dose present in the vaccines. The N2 NA on the recombinant virus was significantly more sensitive to treatment with reducing agent than was the N2 NA on the parent virus. AN antibodies directed against N2 NA on the recombinant differed qualitatively from that directed against N2 NA of parent virus. The results warrant the conclusion that the antigenicity of isolated NA or of NA on recombinant virus can differ from that of the NA on intact homologous virus and that such alterations could influence the determination of antigenic relationship between neuraminidases.
DOI: 10.1007/bf01315632
PubMed: 68766
Links to Exploration step
pubmed:68766Le document en format XML
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Desselberger</name></author></analytic><series><title level="j">Archives of virology</title><idno type="ISSN">0304-8608</idno><imprint><date when="1977" type="published">1977</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Viral (biosynthesis)</term><term>Antigens, Viral (analysis)</term><term>Bromelains (pharmacology)</term><term>Chick Embryo</term><term>Culture Techniques</term><term>Edetic Acid (pharmacology)</term><term>Epitopes</term><term>Guinea Pigs</term><term>Hemagglutinins, Viral (analysis)</term><term>Influenza A virus (analysis)</term><term>Influenza A virus (drug effects)</term><term>Influenza A virus (immunology)</term><term>Mercaptoethanol (pharmacology)</term><term>Neuraminidase (immunology)</term><term>Nitrogen (analysis)</term><term>Recombination, Genetic</term><term>Vaccination</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Antigens, Viral</term><term>Hemagglutinins, Viral</term><term>Nitrogen</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Antibodies, Viral</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Neuraminidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Bromelains</term><term>Edetic Acid</term><term>Mercaptoethanol</term></keywords><keywords scheme="MESH" qualifier="analysis" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Influenza A virus</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>Chick Embryo</term><term>Culture Techniques</term><term>Epitopes</term><term>Guinea Pigs</term><term>Recombination, Genetic</term><term>Vaccination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The influenza virus strains A/Sing/1/57 (H2N2), A/Bel/42 (H0N1) and A/Bel/42 (HO)-A/Sing/1/57 (N2) were treated with bromelain under reducing conditions and with reducing agent alone, and the antigenicity of the neuraminidase (NA) of intact virus and of the split products was tested comparatively. It was found that the antigenicity of NA was influenced quantitatively and qualitatively by the preparation procedure. Antineuraminidase (AN) antibodies obtained after vaccination of guinea pigs with intact virus and with split products differed in their cross-reactivity with heterologous neuraminidases. In several cases, the quantity of AN antibody formation depended on the hemagglutinin (HA) dose present in the vaccines. The N2 NA on the recombinant virus was significantly more sensitive to treatment with reducing agent than was the N2 NA on the parent virus. AN antibodies directed against N2 NA on the recombinant differed qualitatively from that directed against N2 NA of parent virus. The results warrant the conclusion that the antigenicity of isolated NA or of NA on recombinant virus can differ from that of the NA on intact homologous virus and that such alterations could influence the determination of antigenic relationship between neuraminidases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">68766</PMID><DateCompleted><Year>1977</Year><Month>07</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0304-8608</ISSN><JournalIssue CitedMedium="Print"><Volume>53</Volume><Issue>4</Issue><PubDate><Year>1977</Year></PubDate></JournalIssue><Title>Archives of virology</Title><ISOAbbreviation>Arch. Virol.</ISOAbbreviation></Journal><ArticleTitle>Preparation-conditioned changes of the antigenicity of influenza virus neuraminidases.</ArticleTitle><Pagination><MedlinePgn>335-49</MedlinePgn></Pagination><Abstract><AbstractText>The influenza virus strains A/Sing/1/57 (H2N2), A/Bel/42 (H0N1) and A/Bel/42 (HO)-A/Sing/1/57 (N2) were treated with bromelain under reducing conditions and with reducing agent alone, and the antigenicity of the neuraminidase (NA) of intact virus and of the split products was tested comparatively. It was found that the antigenicity of NA was influenced quantitatively and qualitatively by the preparation procedure. Antineuraminidase (AN) antibodies obtained after vaccination of guinea pigs with intact virus and with split products differed in their cross-reactivity with heterologous neuraminidases. In several cases, the quantity of AN antibody formation depended on the hemagglutinin (HA) dose present in the vaccines. The N2 NA on the recombinant virus was significantly more sensitive to treatment with reducing agent than was the N2 NA on the parent virus. AN antibodies directed against N2 NA on the recombinant differed qualitatively from that directed against N2 NA of parent virus. The results warrant the conclusion that the antigenicity of isolated NA or of NA on recombinant virus can differ from that of the NA on intact homologous virus and that such alterations could influence the determination of antigenic relationship between neuraminidases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Desselberger</LastName><ForeName>U</ForeName><Initials>U</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Austria</Country><MedlineTA>Arch Virol</MedlineTA><NlmUniqueID>7506870</NlmUniqueID><ISSNLinking>0304-8608</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000914">Antibodies, 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