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

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

Scientific reports (2020-03-27)
Nan Jia, Lauren Byrd-Leotis, Yasuyuki Matsumoto, Chao Gao, Alexander N Wein, Jenna L Lobby, Jacob E Kohlmeier, David A Steinhauer, Richard D Cummings
摘要

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-]n 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.

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ProteoMass 肽和 蛋白质 MALDI-MS 校准试剂盒, Peptide and Protein MALDI MS Calibration Standard