Isolation of hemagglutination-defective mutants for the analysis of the sialic acid binding activity of transmissible gastroenteritis virus.
The surface protein S of transmissible gastroenteritis virus (TGEV) has a sialic acid binding activity that enables the virus to agglutinate erythrocytes. A protocol is described that has been successfully applied to the isolation of hemgglutination-defective mutants. The potential of these mutants for the characterization of the sialic acid-binding site and the function of the binding activity is discussed.
Institut für Virologie Philipps-Universität Marburg, Germany.
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Krempl
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Ballesteros
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Enjuanes
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G
Herrler
D000818:Animals; D003673:Defective Viruses / Q000302:isolation & purification* / Q000378:metabolism; D006387:Hemagglutination, Viral; D009154:Mutation; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D013552:Swine; D005760:Transmissible gastroenteritis virus / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism
D019158:N-Acetylneuraminic Acid