5bnp
Crystal structure of human enterovirus D68 in complex with 3'SLNCrystal structure of human enterovirus D68 in complex with 3'SLN
Structural highlights
Publication Abstract from PubMedHuman 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. Sialic acid-dependent cell entry of human enterovirus D68.,Liu Y, Sheng J, Baggen J, Meng G, Xiao C, Thibaut HJ, van Kuppeveld FJ, Rossmann MG Nat Commun. 2015 Nov 13;6:8865. doi: 10.1038/ncomms9865. PMID:26563423[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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