Transfer of an esterase-resistant receptor analog to the surface of influenza C virions results in reduced infectivity due to aggregate formation.

@article{Hofling1996TransferOA,
  title={Transfer of an esterase-resistant receptor analog to the surface of influenza C virions results in reduced infectivity due to aggregate formation.},
  author={Katja Höfling and Reinhard Brossmer and Hans Dieter Klenk and Georg Herrler},
  journal={Virology},
  year={1996},
  volume={218 1},
  pages={
          127-33
        }
}
A synthetic sialic acid, N-acetyl-9-thioacetamidoneuraminic acid (9-ThioAcNeu5Ac), is recognized by influenza C virus as a receptor determinant but-in contrast to the natural receptor determinant, N-acetyl-9-O-acetylneuraminic acid-is resistant to inactivation by the viral acetylesterase. This sialic acid analog was used to analyze the importance of the receptor-destroying enzyme of influenza C virus in keeping the viral surface free of receptor determinants. Enzymatic transfer of 9… 
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