Literature DB >> 1645138

Immunoelectron microscopy of influenza A virus neuraminidase glycoprotein topography.

H Amano1, H Uemoto, K Kuroda, Y Hosaka.   

Abstract

Using immunoelectron microscopy, the distribution of influenza A virus neuraminidase (NA) glycoproteins was examined, after performing immunoreactions to virions on the grid. With polyclonal antibody, the immunolabels of the glycoproteins were found to be homogeneously distributed, whereas with monoclonal antibody they were found to be distributed in clusters. After destruction of haemagglutinin (HA) but not of NA activity with a high concentration of trypsin, the remaining visible spikes were evenly distributed. This finding was consistent with the absence of immunolabelling with anti-HA antibody, and the homogeneous pattern of immunolabels with anti-NA polyclonal antibody, but not with the clustered labelling with the anti-NA monoclonal antibody. Thus, the immunolabelling image with anti-NA polyclonal antibody was considered to reflect the true one.

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Year:  1992        PMID: 1645138     DOI: 10.1099/0022-1317-73-8-1969

Source DB:  PubMed          Journal:  J Gen Virol        ISSN: 0022-1317            Impact factor:   3.891


  2 in total

1.  Dissociation of influenza virus hemagglutinin and neuraminidase eliminates their intravirionic antigenic competition.

Authors:  B E Johansson; E D Kilbourne
Journal:  J Virol       Date:  1993-10       Impact factor: 5.103

2.  Bifunctional thiosialosides inhibit influenza virus.

Authors:  Yang Yang; Yun He; Xingzhe Li; Hieu Dinh; Suri S Iyer
Journal:  Bioorg Med Chem Lett       Date:  2013-12-11       Impact factor: 2.823

  2 in total

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