Glycan-mediated enhancement of reovirus receptor binding

Melanie Koehler, Pavithra Aravamudhan, Camila Guzman-Cardozo, Andra C. Dumitru, Jinsung Yang, Serena Gargiulo, Patrice Soumillion, Terence S. Dermody () and David Alsteens ()
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Melanie Koehler: Université catholique de Louvain
Pavithra Aravamudhan: University of Pittsburgh School of Medicine
Camila Guzman-Cardozo: University of Pittsburgh School of Medicine
Andra C. Dumitru: Université catholique de Louvain
Jinsung Yang: Université catholique de Louvain
Serena Gargiulo: Université catholique de Louvain
Patrice Soumillion: Université catholique de Louvain
Terence S. Dermody: University of Pittsburgh School of Medicine
David Alsteens: Université catholique de Louvain

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: Abstract Viral infection is an intricate process that requires the concerted action of both viral and host cell components. Entry of viruses into cells is initiated by interactions between viral proteins and their cell surface receptors. Despite recent progress, the molecular mechanisms underlying the multistep reovirus entry process are poorly understood. Using atomic force microscopy, we investigated how the reovirus σ1 attachment protein binds to both α-linked sialic acid (α-SA) and JAM-A cell-surface receptors. We discovered that initial σ1 binding to α-SA favors a strong multivalent anchorage to JAM-A. The enhanced JAM-A binding by virions following α-SA engagement is comparable to JAM-A binding by infectious subvirion particles (ISVPs) in the absence of α-SA. Since ISVPs have an extended σ1 conformer, this finding suggests that α-SA binding triggers a conformational change in σ1. These results provide new insights into the function of viral attachment proteins in the initiation of infection and open new avenues for the use of reoviruses as oncolytic agents.

Date: 2019
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DOI: 10.1038/s41467-019-12411-2

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