Preparation-conditioned changes of the antigenicity of influenza virus neuraminidases
Identifieur interne : 000C99 ( Istex/Curation ); précédent : 000C98; suivant : 000D00Preparation-conditioned changes of the antigenicity of influenza virus neuraminidases
Auteurs : U. Desselberger [Allemagne]Source :
- Archives of Virology [ 0304-8608 ] ; 1977-12-01.
English descriptors
- Teeft :
- Academic press, Acua, Antibody, Antibody formation, Antibody response, Antibody titers, Antibody titrations, Antigenic, Antigenic relationship, Antigenic variation, Antigenicity, Antineuraminidase, Antineuraminidase antibodies, Antineuraminidase antibody response, Antiserum, Different strains, Enzyme inhibition test, Guinea pigs, Hemagglutination inhibition, Hemagglutinin, Higher degree, Host components, Immunol, Influenza, Influenza virus, Influenza virus neuraminidase, Influenza virus neuraminidases, Influenza virus strain, Influenza virus strains, Influenza viruses, Influenzavirus neuraminidases, Intact virus, Intact virus particles, Laver, Medizinische hochschule hannover, Neuraminidase, Neuraminidases, Nitrogen content, Parent strain, Parent virus, Photometric, Photometric methods, Preparation procedure, Reactivity constants, Recombinant, Recombinant strain, Recombinant virus, Split products, Statistical methods, Subunit, Supernatant fraction, Vaccination, Vaccine, Virol, Virology, Virus, Virus antisera, Virus strains.
Abstract
Summary: The influenza virus strains A/Sing/1/57 (H2N2), A/Bel/42 (H0N1) and A/Bel/42 (H0)-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.
Url:
DOI: 10.1007/BF01315632
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<term>Antigenic relationship</term>
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<term>Reactivity constants</term>
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<front><div type="abstract" xml:lang="en">Summary: The influenza virus strains A/Sing/1/57 (H2N2), A/Bel/42 (H0N1) and A/Bel/42 (H0)-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>
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