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[Detection of the virus-specific proteins of the tick-borne encephalitis virus by immunosorption]
The use of immunosorption of tick-borne encephalitis (TBE) virus preparations on polyspecific antibodies covalently bound with sepharose permits good identification of virus-specific protein synthesis in cell cultures in acute and latent infection. Immune affinity separation of virus-specific proteins p93, p79, p69, p53 (V3), p24, p23, p21, p18, and p13 (NVI 1/2) attests to the high polyspecificity of the employed immune preparation, a hyperimmune anti-TBE horse serum gamma-globulin. From a virion antigen preparation, structural V3 (E) protein is isolated but not other structural proteins, V2 (C) or V1 (M). p93 protein (NV5) is one of the proteins recovered from preparations of nonvirion ("soluble") antigen (NA) alongside with heterogeneous p80 protein which may represent a product of p93 protein proteolysis or protein(s) of pig embryo kidney cells separated in immunosorption together with p93 within HA.
The use of immunosorption of tick-borne encephalitis (TBE) virus preparations on polyspecific antibodies covalently bound with sepharose permits good identification of virus-specific protein synthesis in cell cultures in acute and latent infection. Immune affinity separation of virus-specific proteins p93, p79, p69, p53 (V3), p24, p23, p21, p18, and p13 (NVI 1/2) attests to the high polyspecificity of the employed immune preparation, a hyperimmune anti-TBE horse serum gamma-globulin. From a virion antigen preparation, structural V3 (E) protein is isolated but not other structural proteins, V2 (C) or V1 (M). p93 protein (NV5) is one of the proteins recovered from preparations of nonvirion ("soluble") antigen (NA) alongside with heterogeneous p80 protein which may represent a product of p93 protein proteolysis or protein(s) of pig embryo kidney cells separated in immunosorption together with p93 within HA.
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