AI Article Synopsis
- - Human lung cells have natural binding sites for influenza virus hemagglutinin, primarily featuring the sugar Neu5Ac linked to galactose, which is crucial for the virus's attachment.
- - Neu5Gc, a sugar not usually produced by humans, can enter human cells through diet, and it impacts how hemagglutinin interacts with cells.
- - A study developed six trisaccharides using Neu5Ac and Neu5Gc to analyze their effects on influenza infection, finding that those capped with Neu5Gc were more effective at inhibiting the virus than those with Neu5Ac.
Article Abstract
Human lung epithelial cells natively offer terminal N-acetylneuraminic acid (Neu5Ac) α(2→6)-linked to galactose (Gal) as binding sites for influenza virus hemagglutinin. N-Glycolylneuraminic acid (Neu5Gc) in place of Neu5Ac is known to affect hemagglutinin binding in other species. Not normally generated by humans, Neu5Gc may find its way to human cells from dietary sources. To compare their influence in influenza virus infection, six trisaccharides with Neu5Ac or Neu5Gc α(2→6) linked to Gal and with different reducing end sugar units were prepared using one-pot assembly and divergent transformation. The sugar assembly made use of an N-phthaloyl-protected sialyl imidate for chemoselective activation and α-stereoselective coupling with a thiogalactoside. Assessment of cytopathic effect showed that the Neu5Gc-capped trisaccharides inhibited the viral infection better than their Neu5Ac counterparts.
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| http://dx.doi.org/10.1002/anie.201309646 | DOI Listing |
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