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

Citation:

Jia N, Byrd-Leotis L, Matsumoto Y, Gao C, Wein AN, Lobby JL, Kohlmeier JE, Steinhauer DA, Cummings RD. The Human Lung Glycome Reveals Novel Glycan Ligands for Influenza A Virus. Sci Rep. 2020;10 (1) :5320.

Date Published:

2020 03 24

Abstract:

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.