Sialic acid-dependent cell entry of human enterovirus D68

Yue Liu, Ju Sheng, Jim Baggen, Geng Meng, Chuan Xiao, Hendrik J. Thibaut, Frank J. M. van Kuppeveld and Michael G. Rossmann ()
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Yue Liu: Hockmeyer Hall of Structural Biology, 240 South Martin Jischke Drive, Purdue University
Ju Sheng: Hockmeyer Hall of Structural Biology, 240 South Martin Jischke Drive, Purdue University
Jim Baggen: Faculty of Veterinary Medicine, Utrecht University
Geng Meng: Hockmeyer Hall of Structural Biology, 240 South Martin Jischke Drive, Purdue University
Chuan Xiao: University of Texas at El Paso, 500 W. University Avenue
Hendrik J. Thibaut: Faculty of Veterinary Medicine, Utrecht University
Frank J. M. van Kuppeveld: Faculty of Veterinary Medicine, Utrecht University
Michael G. Rossmann: Hockmeyer Hall of Structural Biology, 240 South Martin Jischke Drive, Purdue University

Nature Communications, 2015, vol. 6, issue 1, 1-7

Abstract: Abstract Human enterovirus D68 (EV-D68) is a causative agent of childhood respiratory diseases and has now emerged as a global public health threat. Nevertheless, knowledge of the tissue tropism and pathogenesis of EV-D68 has been hindered by a lack of studies on the receptor-mediated EV-D68 entry into host cells. Here we demonstrate that cell surface sialic acid is essential for EV-D68 to bind to and infect susceptible cells. Crystal structures of EV-D68 in complex with sialylated glycan receptor analogues show that they bind into the ‘canyon’ on the virus surface. The sialic acid receptor induces a cascade of conformational changes in the virus to eject a fatty-acid-like molecule that regulates the stability of the virus. Thus, virus binding to a sialic acid receptor and to immunoglobulin-like receptors used by most other enteroviruses share a conserved mechanism for priming viral uncoating and facilitating cell entry.

Date: 2015
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DOI: 10.1038/ncomms9865

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