Investigating the Interaction Between Influenza and Sialic Acid: Making and Breaking the Link

Part of the Milestones in Drug Therapy book series (MDT)


Since the early 1940s sialic acid (Sia) has been regarded as the primary receptor for influenza virus. This Sia is usually bound to an adjacent galactose (Gal) in an α2-3 or α2-6 configuration. This led to a concept about an interspecies barrier as avian viruses preferentially bind to Sia α2-3 linked to Gal, whereas human viruses have a preference for the Sia α2-6 linked to Gal and that transmission from one species to another would preferentially occur only in a host species in which both types of Sia were present. The viral haemagglutinin binds to Sia to facilitate cellular entry. To release progeny viral particles the second main component of the influenza viral envelope – neuraminidase, cleaves Sia. The viral-receptor interaction was initially investigated using agglutination of red blood cells and later using lectin histochemistry. Recent techniques investigating the HA-Sia/NA-Sia link have employed the use of glycan arrays and virus-like pseudoparticles with STD-NMR.


Influenza Virus Sialic Acid Glycan Chain Lectin Histochemistry Avian Virus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



Research supported by funding from Wellcome Trust, UK (082098, 081184/Z/06/Z), Research Grants Committee (GRF 4774109), HKSAR and Research Fund for Control of Infectious Disease (08070842), Government of HKSAR, NIAID. Drs Stuart Haslam and Rositsa Karamanska, Imperial College, United Kingdom are thanked for valuable help on glycan structures and glycobiology experience.


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Copyright information

© Springer Basel AG 2012

Authors and Affiliations

  • John M. Nicholls
    • 1
  • Jimmy Lai
    • 2
  • Jean-Michel Garcia
    • 2
  1. 1.Department of PathologyThe University of Hong KongPok Fu LamHong Kong
  2. 2.HKU-Pasteur Research CentreThe University of Hong KongPok Fu LamHong Kong

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