The “human influenza receptor” Neu5Acα2,6Gal is expressed among different taxa of wild birds

The “human influenza receptor” Neu5Acα2,6Gal is expressed among different taxa of wild birds 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 [1] 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 [22]). 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

The “human influenza receptor” Neu5Acα2,6Gal is expressed among different taxa of wild birds

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Publisher
Springer Journals
Copyright
Copyright © 2009 by Springer-Verlag
Subject
Biomedicine; Infectious Diseases; Medical Microbiology ; Virology
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-009-0476-8
Publisher site
See Article on Publisher Site

Abstract

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 [1] 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 [22]). 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

Journal

Archives of VirologySpringer Journals

Published: Sep 1, 2009

References

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