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Journal ArticleDOI

Selection and analysis of antigenic variants of the neuraminidase of N2 influenza viruses with monoclonal antibodies

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TLDR
Analysis of field strains showed that antigenic variation in the neuraminidase was evident even between influenza virus isolated in the first year following the emergence of a new pandemic strain, suggesting that the distribution of neuramidase molecules may differ among viruses possessing N2 neuraminidsase.
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This article is published in Virology.The article was published on 1982-02-01. It has received 103 citations till now. The article focuses on the topics: Neuraminidase & Antigenic drift.

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Citations
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Journal ArticleDOI

Evolution and ecology of influenza A viruses.

TL;DR: Wild aquatic bird populations have long been considered the natural reservoir for influenza A viruses with virus transmission from these birds seeding other avian and mammalian hosts, but recent studies in bats have suggested other reservoir species may also exist.
Journal ArticleDOI

Structure of the catalytic and antigenic sites in influenza virus neuraminidase

TL;DR: The catalytic sites of influenza virus neuraminidase are located on the upper corners of the box-shaped tetramer that forms the head of the molecule, and determinants form a nearly-continuous surface across the top of the monomer encircling the catalytic site.
Journal ArticleDOI

Influenza virus neuraminidase: structure, antibodies, and inhibitors.

Peter M. Colman
- 01 Oct 1994 - 
TL;DR: The determination of the 3‐dimensional structure of the influenza virus neuraminidase in 1983 has served as a platform for understanding interactions between antibodies and protein antigens, for investigating antigenic variation in influenza viruses, and for devising new inhibitors of the enzyme.
Journal ArticleDOI

Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies.

TL;DR: To analyze the pathogenesis of the neurotropic murine coronavirus JHMV, monoclonal antibodies to the E2 viral glycoprotein were used to select antigenic variant viruses and demyelinating variants with reduced neurovirulence were selected.
Journal ArticleDOI

The neuraminidase of influenza virus.

TL;DR: The crystal structure of influenza virus neuraminidase is described, information about the active site which may lead to development of specific and effective inhibitors of the enzyme, and the structure of epitopes (antigenic determinants) on the neuraminidsase are described.
References
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Derivation of specific antibody-producing tissue culture and tumor lines by cell fusion

TL;DR: Cell fusion techniques have been used to produce hybrids between myeloma cells and antibody‐producing cells that are permanently adapted to grow in tissue culture and are capable of inducing antibody-producing tumors in mice.
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A better cell line for making hybridomas secreting specific antibodies

TL;DR: The identification of such a cell line, Sp2/0-Ag14, is reported here the identification of a tumour cell fusion partner that makes no Ig but which can nevertheless be fused with spleen cells to obtain hybrids secreting only the specific antibody.
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Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation

TL;DR: Four ‘antigenic sites’ on the three-dimensional structure of the influenza haemagglutinin are identified and at least one amino acid substitution in each site seems to be required for the production of new epidemic strains between 1968 and 1975.
Journal ArticleDOI

Characterization of temperature sensitive influenza virus mutants defective in neuraminidase.

TL;DR: The results suggest that the lack of hemagglutinating activity of mutant virus grown at 39.5° is a consequence of the formation of aggregates of virus particles carrying neuraminic acid on their surface, and that the ts defect is in the neuraminidase but not the hemagGLutinin molecule.
Journal Article

Influenzavirus neuraminidase and neuraminidase-inhibition test procedures.

TL;DR: The neuraminidase-inhibition test, as performed in the two WHO international reference centres for influenza, is described and its use in other laboratories-particularly those collaborating in the WHO programme-is recommended.
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