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Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein

2017; National Academy of Sciences; Volume: 114; Issue: 40 Linguagem: Inglês

10.1073/pnas.1712592114

1091-6490

Wentao Li, Ruben J. G. Hulswit, Ivy Widjaja, V. Stalin Raj, Ryan McBride, Wenjie Peng, W. Widagdo, M. Alejandra Tortorici, Brenda van Dieren, Yifei Lang, J.W.M. van Lent, James C. Paulson, Cornelis A. M. de Haan, Raoul J. de Groot, Frank J. M. van Kuppeveld, Bart L. Haagmans, Berend‐Jan Bosch,

Viral gastroenteritis research and epidemiology

Significance Middle East respiratory syndrome coronavirus (MERS-CoV) recurrently infects humans from its dromedary camel reservoir, causing severe respiratory disease with an ∼35% fatality rate. The virus binds to the dipeptidyl peptidase 4 (DPP4) entry receptor on respiratory epithelial cells via its spike protein. We here report that the MERS-CoV spike protein selectively binds to sialic acid (Sia) and demonstrate that cell-surface sialoglycoconjugates can serve as an attachment factor. Our observations warrant further research into the role of Sia binding in the virus’s host and tissue tropism and transmission, which may be influenced by the observed Sia-binding fine specificity and by differences in sialoglycomes among host species.