Abstract
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.
Published Version
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