Is the sialic acid binding activity of the S protein involved in the enteropathogenicity of transmissible gastroenteritis virus?
Transmissible gastroenteritis virus (TGEV) is able to recognize sialic acid on sialo-glycoconjugates. Analysis of mutants indicated that single point mutations in the S protein (around amino acids 145-155) of TGEV may result both in the loss of the sialic acid binding activity and in a drastic reduction of the enteropathogenicity. From this observation we conclude that the sialic acid binding activity is involved in the enteropathogenicity of TGEV. On the basis of our recent results we propose that binding of sialylated macromolecules to the virions surface may increase virus stability. This in turn would explain how TGEV as an enveloped virus can survive the gastrointestinal passage and cause intestinal infections.
Institut für Virologie Philipps-Universität Marburg, Germany.
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Krempl
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Laude
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Herrler
D000818:Animals; D005759:Gastroenteritis / Q000662:veterinary* / Q000821:virology; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D064370:Spike Glycoprotein, Coronavirus; D013552:Swine; D013553:Swine Diseases / Q000821:virology*; D005760:Transmissible gastroenteritis virus / Q000378:metabolism / Q000472:pathogenicity*; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*
D008562:Membrane Glycoproteins; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins; C578557:spike glycoprotein, SARS-CoV; C578553:spike protein, mouse hepatitis virus; D019158:N-Acetylneuraminic Acid