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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, Jahrgang 5, Nr. 2, eaav2554, 02.2019.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Byrd-Leotis, L, Jia, N, Dutta, S, Trost, JF, Gao, C, Cummings, SF, Braulke, T, Müller-Loennies, S, Heimburg-Molinaro, J, Steinhauer, DA & Cummings, RD 2019, 'Influenza binds phosphorylated glycans from human lung', SCI ADV, Jg. 5, Nr. 2, eaav2554. https://doi.org/10.1126/sciadv.aav2554

APA

Byrd-Leotis, L., Jia, N., Dutta, S., Trost, J. F., Gao, C., Cummings, S. F., Braulke, T., Müller-Loennies, S., Heimburg-Molinaro, J., Steinhauer, D. A., & Cummings, R. D. (2019). Influenza binds phosphorylated glycans from human lung. SCI ADV, 5(2), [eaav2554]. https://doi.org/10.1126/sciadv.aav2554

Vancouver

Byrd-Leotis L, Jia N, Dutta S, Trost JF, Gao C, Cummings SF et al. Influenza binds phosphorylated glycans from human lung. SCI ADV. 2019 Feb;5(2). eaav2554. https://doi.org/10.1126/sciadv.aav2554

Bibtex

@article{585ce9c316ac4a31b7c82d35adef3f5c,
title = "Influenza binds phosphorylated glycans from human lung",
abstract = "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.",
keywords = "Animals, Chromatography, High Pressure Liquid, Humans, Influenza A virus/physiology, Influenza, Human/metabolism, Lung/metabolism, Mass Spectrometry, Phosphorylation, Polysaccharides/chemistry, Proteomics/methods, Viral Proteins",
author = "Lauren Byrd-Leotis and Nan Jia and Sucharita Dutta and Trost, {Jessica F} and Chao Gao and Cummings, {Sandra F} and Thomas Braulke and Sven M{\"u}ller-Loennies and Jamie Heimburg-Molinaro and Steinhauer, {David A} and Cummings, {Richard D}",
year = "2019",
month = feb,
doi = "10.1126/sciadv.aav2554",
language = "English",
volume = "5",
journal = "SCI ADV",
issn = "2375-2548",
publisher = "American Association for the Advancement of Science",
number = "2",

}

RIS

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 -