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Updated: Apr 23, 2026
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A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
Published on: May 29, 2016
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Paramyxovirus infection driven by heteromultivalent sialoglycotope binding.
Xuesheng Wu1, Mengying Liu1, Laura Blekkenhorst1
1Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University, Utrecht 3584CL, the Netherlands.
Summary
Respirovirus infection requires sialic acids (Sia) linked via α2-3 (2-3Sia), preferring a specific terminal glycan. Interestingly, 2-6Sia enhances infection by prolonging virus-receptor interactions in the upper respiratory tract.
Area of Science:
- Virology
- Glycobiology
- Cell Biology
Background:
- Sialic acids (Sia) on cell surfaces serve as critical attachment receptors for numerous respiratory viruses.
- Viruses like influenza A and respiroviruses bind to specific Sia linkages (α2-6 and α2-3, respectively), but respirovirus receptor requirements are not fully understood.
Purpose of the Study:
- To elucidate the precise sialoglycoconjugate requirements for respirovirus and Newcastle disease virus (NDV) infection and binding.
- To investigate the role of different Sia linkages in supporting viral entry.
Main Methods:
- Utilized a library of isogenic HEK293 cells engineered to display specific sialoglycoconjugates.
- Assessed viral binding and infection efficiency of respiroviruses and NDV on these engineered cells.
Main Results:
- Respirovirus infection strictly depends on α2-3-linked Sia (2-3Sia), with a preference for the Siaα2-3Galβ1-4GlcNAc glycan.
- Newcastle disease virus (NDV) demonstrated broader sialoglycotope usage compared to respiroviruses.
- α2-6-linked Sia (2-6Sia) was found to enhance respirovirus infection in low 2-3Sia environments through heteromultivalent binding, prolonging virus-receptor interactions.
Conclusions:
- Respirovirus tropism is dictated by the presence of 2-3Sia, particularly the Siaα2-3Galβ1-4GlcNAc structure.
- Heteromultivalent binding involving 2-6Sia may facilitate respirovirus infection in the human upper respiratory tract, which is rich in 2-6Sia.
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