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    Article

    Sequence variation and biological activity of rubella virus isolates

    Haemagglutination (HA) by rubella virus is mediated by the E1 glycoprotein. Rubella isolates which haemagglutinate with different avidity have been characterised. A significant reduction of HA titre at pH6.0 w...

    P. Londesborough, L. Ho-Terry, G. Terry in Archives of Virology (1995)

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    Article

    Reactivity of a recombinant rubella E1 antigen expressed inE. coli

    The E1 nucleic acid sequence of rubella virus strain Judith (RJ) has been cloned into anE. coli expression vector LB03. The reactivity of the expressed unglycosylated antigen (E1J) was compared with its glycosyla...

    P. Londesborough, G. Terry, L. Ho-Terry in Archives of Virology (1992)

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    Article

    A bio-engineered rubella E1 antigen

    The major rubella envelope protein, E1, and a segment of it, comprising amino acids 207–353, have been separately expressed as fusion proteins with the IgG binding region ofStaphylococcus aureus protein A inEsche...

    G. M. Terry, L. Ho-Terry, P. Londesborough, K. R. Rees in Archives of Virology (1989)

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    Article

    Localization of the rubella E1 epitopes

    Three epitopes which react with haemagglutination inhibition and neutralizing antibodies have been located between amino acids 245–285 in the predicted amino acid sequence of rubella envelope glycoprotein E1.

    G. M. Terry, L. Ho-Terry, P. Londesborough, K. R. Rees in Archives of Virology (1988)

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    Article

    Rubella virus RNA: Effect of high multiplicity passage

    Evidence for the amplification of defective interfering particles of rubella virus after passage at high multiplicity has been obtained. The process is associated with the production of subgenomic rubella RNA ...

    G. M. Terry, L. Ho-Terry, A. Cohen, P. Londesborough in Archives of Virology (1985)

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    Article

    Fusion and haemolysis of chick erythrocytes by Newcastle disease virus

    An avirulent strain of Newcastle disease virus has been shown to be capable of causing fusion of chick erythrocytes.

    G. M. Terry, L. Ho-Terry in Archives of Virology (1976)