Influenza binds phosphorylated glycans from human lung
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Influenza binds phosphorylated glycans from human lung. / Byrd-Leotis, Lauren; Jia, Nan; Dutta, Sucharita; Trost, Jessica F; Gao, Chao; Cummings, Sandra F; Braulke, Thomas; Müller-Loennies, Sven; Heimburg-Molinaro, Jamie; Steinhauer, David A; Cummings, Richard D.
In: SCI ADV, Vol. 5, No. 2, eaav2554, 02.2019.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Influenza binds phosphorylated glycans from human lung
AU - Byrd-Leotis, Lauren
AU - Jia, Nan
AU - Dutta, Sucharita
AU - Trost, Jessica F
AU - Gao, Chao
AU - Cummings, Sandra F
AU - Braulke, Thomas
AU - Müller-Loennies, Sven
AU - Heimburg-Molinaro, Jamie
AU - Steinhauer, David A
AU - Cummings, Richard D
PY - 2019/2
Y1 - 2019/2
N2 - Influenza A viruses can bind sialic acid-terminating glycan receptors, and species specificity is often correlated with sialic acid linkage with avian strains recognizing α2,3-linked sialylated glycans and mammalian strains preferring α2,6-linked sialylated glycans. These paradigms derive primarily from studies involving erythrocyte agglutination, binding to synthetic receptor analogs or binding to undefined surface markers on cells or tissues. Here, we present the first examination of the N-glycome of the human lung for identifying natural receptors for a range of avian and mammalian influenza viruses. We found that the human lung contains many α2,3- and α2,6-linked sialylated glycan determinants bound by virus, but all viruses also bound to phosphorylated, nonsialylated glycans.
AB - Influenza A viruses can bind sialic acid-terminating glycan receptors, and species specificity is often correlated with sialic acid linkage with avian strains recognizing α2,3-linked sialylated glycans and mammalian strains preferring α2,6-linked sialylated glycans. These paradigms derive primarily from studies involving erythrocyte agglutination, binding to synthetic receptor analogs or binding to undefined surface markers on cells or tissues. Here, we present the first examination of the N-glycome of the human lung for identifying natural receptors for a range of avian and mammalian influenza viruses. We found that the human lung contains many α2,3- and α2,6-linked sialylated glycan determinants bound by virus, but all viruses also bound to phosphorylated, nonsialylated glycans.
KW - Animals
KW - Chromatography, High Pressure Liquid
KW - Humans
KW - Influenza A virus/physiology
KW - Influenza, Human/metabolism
KW - Lung/metabolism
KW - Mass Spectrometry
KW - Phosphorylation
KW - Polysaccharides/chemistry
KW - Proteomics/methods
KW - Viral Proteins
U2 - 10.1126/sciadv.aav2554
DO - 10.1126/sciadv.aav2554
M3 - SCORING: Journal article
C2 - 30788437
VL - 5
JO - SCI ADV
JF - SCI ADV
SN - 2375-2548
IS - 2
M1 - eaav2554
ER -