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


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) [-3Gal?1-4GlcNAc?1-]n extensions, which are predominantly terminated in ?2,3-linked sialic acid. By contrast, smaller N-glycans lack PL and are enriched in ?2,6-linked sialic acids. In addition, we observed large glycosphingolipid (GSL)-glycans, which also consists of linear PL, terminating in mainly ?2,3-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.

SUBMITTER: Jia N 

PROVIDER: S-EPMC7093477 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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

Jia Nan N   Byrd-Leotis Lauren L   Matsumoto Yasuyuki Y   Gao Chao C   Wein Alexander N AN   Lobby Jenna L JL   Kohlmeier Jacob E JE   Steinhauer David A DA   Cummings Richard D RD  

Scientific reports 20200324 1


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-]<sub>n</sub> extensions, which are predominantly terminated in α2,3-li  ...[more]

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