Arch Virol (2009) 154:1533–1537 DOI 10.1007/s00705-009-0476-8 BRIEF REPORT The ‘‘human inﬂuenza receptor’’ Neu5Aca2,6Gal is expressed among different taxa of wild birds Patrik Ellstro ¨ m Æ Elsa Jourdain Æ Oskar Gunnarsson Æ Jonas Waldenstro ¨ m Æ Bjo ¨ rn Olsen Received: 22 April 2009 / Accepted: 13 July 2009 / Published online: 9 August 2009 Springer-Verlag 2009 Inﬂuenza A viruses (IAVs) bind glycoconjugate receptors Accordingly, a2,6-sialylated glycans have been found in displaying terminal sialic acids on host cells. The virus the tracheae of humans  and a2,3-sialylated glycans in hemagglutinin (HA) protein mediates adhesion to the the intestines of mallards (Anas plathyrhyncos), chickens cells via the core structure ‘‘Neu5Aca2,3(6)Galb1,3(4)Glc- (Gallus gallus) and quails (Coturnix japonica)[7, 9–11, 23]. NAcb1-’’ where the linkage between the sialic acid and the Based on these results, the Neu5Aca2,3Gal structure galactose can be either a2,3 or a2,6 (reviewed by Suzuki was termed the ‘‘avian inﬂuenza receptor’’, whereas the ). Adhesion to these structures is a crucial ﬁrst step in Neu5Aca2,6Gal structure was denoted the ‘‘human inﬂu- the infection process, and several studies have shown that enza receptor’’ [8, 26]. However, poultry isolates with the linkage between the sialic acids and the galactose is a
Archives of Virology – Springer Journals
Published: Sep 1, 2009
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