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Published ahead of print on December 12, 2003, doi:10.1165/rcmb.2003-0355OC

Am. J. Respir. Cell Mol. Biol., Volume 30, Number 6, June 2004, 871-879

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Submitted on October 1, 2003
Revised on December 12, 2003

Interactions of Influenza A virus with Sialic Acids present on Porcine Surfactant Protein D

Martin van Eijk1*, Mitchell R White2, Joseph J Batenburg1, Arie B Vaandrager1, Lambert M.G. van Golde1, Henk P Haagsman3, and Kevan L Hartshorn2

1 Department of Biochemistry and Cell Biology, Utrecht University, Faculty of Veterinary Medicine, Utrecht, The Netherlands, 2 Department of Medicine, Boston University School of Medicine, Boston, MA, USA, 3 Department of Public Health and Food Safety, Utrecht University, Faculty of Veterinary Medicine, Utrecht, The Netherlands

* To whom correspondence should be addressed. E-mail: m.vaneijk{at}vet.uu.nl.

Pigs can be infected with both human and avian influenza A virus (IAV) strains and are therefore considered to be important intermediates in the emergence of new IAV strains due to mixing of viral genes derived from human, avian or porcine influenza viruses. These reassortant strains may have potential to cause pandemic influenza outbreaks in humans. The innate immune response against IAV plays a significant role in containment of IAV in the airways. We studied the interactions of IAV with porcine surfactant protein D (pSP-D), an important component of this first line defense system. Hemagglutination inhibition analysis shows that the distinct interactions of pSP-D with IAV mediated by the N-linked carbohydrate moiety in the carbohydrate recognition domain of pSP-D, depend on the terminal sialic acids (SAs) present on this carbohydrate. Analysis by both lectin staining and by cleavage with linkage-specific sialidases shows that the carbohydrate of pSP-D is exclusively sialylated with {alpha}(2,6)-linked SAs, in contrast to surfactant protein A which contains both {alpha}(2,3)- and {alpha}(2,6)-linked SAs on its N-linked carbohydrate. Enzymatic modification of the SA-linkages present on pSP-D demonstrates that the type of SA-linkage is important for its hemagglutination inhibitory activity, and correlates with receptor-binding specificity of the IAV strains. The SAs present on pSP-D appear especially important for interactions with poorly glycosylated IAV strains. It remains to be elucidated to what extent the unique sialylation profile of pSP-D is involved in host range control of IAV in pigs and, whether it facilitates adaptation of avian or human IAV strains that can contribute to the production of reassortant strains in pigs.




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