The Human Lung Glycome Reveals Novel Glycan Ligands for Influenza A Virus

Glycans within human lungs are recognized by many pathogens such as influenza A virus (IAV), yet little is known about their structures. Here we present the first analysis of the N- and O- and glycosphingolipid-glycans from total human lungs, along with histological analyses of IAV binding. The N-gl...

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Bibliographic Details
Published in:Scientific reports 2020-03, Vol.10 (1), p.5320-5320, Article 5320
Main Authors: Jia, Nan, Byrd-Leotis, Lauren, Matsumoto, Yasuyuki, Gao, Chao, Wein, Alexander N, Lobby, Jenna L, Kohlmeier, Jacob E, Steinhauer, David A, Cummings, Richard D
Format: Article
Language:English
Subjects:
Binding sites
Binding Sites - physiology
Humans
Influenza
Influenza A
Influenza A virus - metabolism
Influenza A virus - pathogenicity
Influenza, Human - metabolism
Influenza, Human - virology
Lectins
Lectins - metabolism
Ligands
Lung - metabolism
Lung - pathology
Lungs
N-acetyllactosamine
N-glycans
Neuraminidase - pharmacology
Pathogens
Phosphorylation
Poly-N-acetyllactosamine
Polysaccharides
Polysaccharides - chemistry
Polysaccharides - metabolism
Sialic acids
Sialic Acids - metabolism
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Summary:Glycans within human lungs are recognized by many pathogens such as influenza A virus (IAV), yet little is known about their structures. Here we present the first analysis of the N- and O- and glycosphingolipid-glycans from total human lungs, along with histological analyses of IAV binding. The N-glycome of human lung contains extremely large complex-type N-glycans with linear poly-N-acetyllactosamine (PL) [-3Galβ1-4GlcNAcβ1-] extensions, which are predominantly terminated in α2,3-linked sialic acid. By contrast, smaller N-glycans lack PL and are enriched in α2,6-linked sialic acids. In addition, we observed large glycosphingolipid (GSL)-glycans, which also consists of linear PL, terminating in mainly α2,3-linked sialic acid. Histological staining revealed that IAV binds to sialylated and non-sialylated glycans and binding is not concordant with respect to binding by sialic acid-specific lectins. These results extend our understanding of the types of glycans that may serve as binding sites for human lung pathogens.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-020-62074-z