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Book Chapter: Investigating the interaction between influenza and sialic acid : making and breaking the link

TitleInvestigating the interaction between influenza and sialic acid : making and breaking the link
Authors
Issue Date2012
PublisherSpringer
Citation
Investigating the interaction between influenza and sialic acid : making and breaking the link. In Itzstein, MV (Ed.), Influenza virus sialidase : a drug discovery target, p. 31-45. Basel: Springer, 2012 How to Cite?
AbstractSince 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.
Persistent Identifierhttp://hdl.handle.net/10722/166839
ISBN

 

DC FieldValueLanguage
dc.contributor.authorNicholls, JMen_US
dc.contributor.authorLai, JCCen_US
dc.contributor.authorGarcia, JCen_US
dc.date.accessioned2012-09-20T08:51:01Z-
dc.date.available2012-09-20T08:51:01Z-
dc.date.issued2012en_US
dc.identifier.citationInvestigating the interaction between influenza and sialic acid : making and breaking the link. In Itzstein, MV (Ed.), Influenza virus sialidase : a drug discovery target, p. 31-45. Basel: Springer, 2012en_US
dc.identifier.isbn9783764389260en_US
dc.identifier.urihttp://hdl.handle.net/10722/166839-
dc.description.abstractSince 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.-
dc.languageengen_US
dc.publisherSpringeren_US
dc.relation.ispartofInfluenza virus sialidase : a drug discovery targeten_US
dc.titleInvestigating the interaction between influenza and sialic acid : making and breaking the linken_US
dc.typeBook_Chapteren_US
dc.identifier.emailNicholls, JM: jmnichol@hkucc.hku.hken_US
dc.identifier.emailLai, JCC: jimmylcc@hku.hken_US
dc.identifier.emailGarcia, JC: jmgarcia@hku.hken_US
dc.identifier.authorityNicholls, JM=rp00364en_US
dc.identifier.doi10.1007/978-3-7643-8927-7_2-
dc.identifier.hkuros205816en_US
dc.identifier.spage31en_US
dc.identifier.epage45en_US
dc.publisher.placeBasel-
dc.customcontrol.immutableyiu 130924-

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