Paramyxovirus infection driven by heteromultivalent sialoglycotope binding

X Xuesheng Wu (Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University) M Mengying Liu L Laura Blekkenhorst (Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University) M Mare H. L. Verbruggen (Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University) N Nancy N. M. P. Schuurman (Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University) L Lemeng Chao (Department Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University) J Jun Yang Ong (Department Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University) T Tom Wennekes (Department Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University) L Laura L. A. van Dijk (Department of Viroscience, Erasmus University Medical Center) R Rory D. de Vries (Department of Viroscience, Erasmus University Medical Center) F Frank J. M. van Kuppeveld H Henrik Clausen Y Yoshiki Narimatsu E Erik de Vries C Cornelis A. M. de Haan (Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University)

Abstract

Sialic acids (Sia) on glycoproteins and glycosphingolipids act as receptors for many respiratory viruses, including human influenza A viruses and respiroviruses, which typically bind to α2-6- and α2-3-linked Sia (2-6Sia and 2-3Sia), respectively. In view of this binding discrepancy and as the exact sialoglycoconjugates supporting respirovirus infection remain unclear, we assessed the receptor requirements for infection and binding of several respiroviruses and avian Newcastle disease virus (NDV). To this end, we employed a library of isogenic HEK293 cells displaying defined sialoglycoconjugates. Respirovirus infection was shown to strictly depend on 2-3Sia, with a preference for the terminal Siaα2-3Galβ1-4GlcNAc sialoglycotope regardless of the underlying glycoconjugate structure, whereas NDV showed a broader sialoglycotope usage. Notably, 2-6Sia enhanced respirovirus infection in low 2-3Sia contexts via heteromultivalent surface binding, which resulted in prolonged virus–receptor interactions. This heteromultivalent binding is expected to aid respirovirus infection of the 2-6Sia-rich human upper respiratory tract.

Article Details

Volume / Issue Vol. 123, Issue 17
Published April 28, 2026
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (15)

X

Xuesheng Wu

Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University

M

Mengying Liu

L

Laura Blekkenhorst

Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University

M

Mare H. L. Verbruggen

Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University

N

Nancy N. M. P. Schuurman

Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University

L

Lemeng Chao

Department Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University

J

Jun Yang Ong

Department Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University

T

Tom Wennekes

Department Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University

L

Laura L. A. van Dijk

Department of Viroscience, Erasmus University Medical Center

R

Rory D. de Vries

Department of Viroscience, Erasmus University Medical Center

F

Frank J. M. van Kuppeveld

H

Henrik Clausen

Y

Yoshiki Narimatsu

E

Erik de Vries

C

Cornelis A. M. de Haan

Section Virology, Division Infectious Diseases and Immunology, Department Biomolecular Health Sciences, Faculty Veterinary Medicine, Utrecht University