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Nat Commun. 2015 Nov 13;6:8865. doi: 10.1038/ncomms9865.

Sialic acid-dependent cell entry of human enterovirus D68.

Author information

1
Department of Biological Sciences, Hockmeyer Hall of Structural Biology, 240 South Martin Jischke Drive, Purdue University, West Lafayette, Indiana 47907, USA.
2
Department of Infectious Diseases and Immunology, Virology Division, Faculty of Veterinary Medicine, Utrecht University, 3584CL Utrecht, The Netherlands.
3
Department of Chemistry, University of Texas at El Paso, 500 W. University Avenue, El Paso, Texas 79968-0519, USA.

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.

PMID:
26563423
PMCID:
PMC4660200
DOI:
10.1038/ncomms9865
[Indexed for MEDLINE]
Free PMC Article

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