期刊
CHEM
卷 7, 期 12, 页码 3393-3411出版社
CELL PRESS
DOI: 10.1016/j.chempr.2021.09.015
关键词
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资金
- NIH Director's New Innovator Award (NICHD) [1DP2HD087954-01]
- NIH Director's Glycoscience Common Fund [1R21AI129894-01]
- Gordon and Betty Moore Foundation [9162.07]
- Alfred P. Sloan Foundation [FG-2017-9094]
- Research Corporation for Science Advancement via the Cottrell Scholar Award [24119]
- Chemistry and Biology Interface training program (NIGMS) [5T32GM112584-03]
- NSF [MCB-1942763]
- NIH [GM095583]
- DoD National Defense Education Program Center [HQ00342110007]
- ASU-Mayo Foundation
- AstraZenaca
- Arizona State University School of Molecular Sciences and Biodesign Institute's Center for Applied Structural Discovery
- G. Harold and Leyla Y. Mathers Charitable Foundation
- UCSD Paths Program
- Undergraduate Summer Research Award through the UCSD Division of Physical Sciences
- U.S. Department of Defense (DOD) [HQ00342110007] Funding Source: U.S. Department of Defense (DOD)
The study found that host glycan presentation and density can impact IAV virus recognition of specific receptors. Binding of H1N1 and H3N2 to alpha 2,3- and alpha 2,6-sialyllactose receptor arrays revealed different sensitivities to receptor presentation.
Influenza A viruses (IAVs) exploit host glycans in airway mucosa for entry and infection. Detection of changes in IAV glycan-binding phenotype can provide early indication of transmissibility and infection potential. While zoonotic viruses are monitored for mutations, the influence of host glycan presentation on viral specificity remains obscured. Here, we describe an array platform that uses synthetic mimetics of mucin glycoproteins to model how receptor presentation and density in the mutinous glycocalyx may impact IAV recognition H1N1 and H3N2 binding in arrays of alpha 2,3- and alpha 2,6-sialyllactose receptors confirmed their known sialic-acid-binding specificities and revealed their different sensitivities to receptor presentation. Further, the transition of H1N1 from avian to mammalian cell culture improved the ability of the virus to recognize mucin-like displays of alpha 2,6-sialic acid receptors. Support vector machine (SVM) learning efficiently characterized this shift in binding preference and may prove useful to study viral evolution to a new host.
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