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      Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus.

      Journal of Biology
      Animals, Cell Line, Chickens, Hemagglutinins, metabolism, LLC-PK1 Cells, Male, Membrane Glycoproteins, genetics, Neuraminidase, pharmacology, Point Mutation, Receptors, Virus, Sialic Acids, Spike Glycoprotein, Coronavirus, Swine, Transmissible gastroenteritis virus, pathogenicity, Viral Envelope Proteins

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          Abstract

          Enteropathogenic transmissible gastroenteritis virus (TGEV), a porcine coronavirus, is able to agglutinate erythrocytes because of sialic acid binding activity. Competitive inhibitors that may mask the sialic acid binding activity can be inactivated by sialidase treatment of virions. Here, we show that TGEV virions with efficient hemagglutinating activity were also obtained when cells were treated with sialidase prior to infection. This method was used to analyze TGEV mutants for hemagglutinating activity. Recently, mutants with strongly reduced enteropathogenicity that have point mutations or a deletion of four amino acids within residues 145 to 155 of the S protein have been described. Here, we show that in addition to their reduced pathogenicity, these mutants also have lost hemagglutinating activity. These results connect sialic acid binding activity with the enteropathogenicity of TGEV.

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