Abstract：
:A new influenza-like virus genome (H17N10) was recently discovered in bats and offers a new perspective about the origin and evolution of influenza viruses. The viral envelope glycoprotein hemagglutinin (HA) is responsible for influenza virus receptor binding, fusion, and entry into the cell; therefore, the structure and function of HA H17 was characterized. The 2.70 Å resolution crystal structure revealed that H17 has a typical influenza A virus HA fold, but with some special features, including a distorted putative sialic acid (SA) binding site and low thermostability. No binding to either the canonical human α2,6 SA-linkage or avian α2,3 SA-linkage receptor was observed. Furthermore, H17 glycan binding was not detected using a chip covering more than 600 glycans. Our results demonstrate that H17 is unique among characterized HAs and that the bat-derived influenza virus may use a different entry mechanism compared to canonical influenza viruses.
journal_name
Cell Repjournal_title
Cell reportsauthors
Sun X,Shi Y,Lu X,He J,Gao F,Yan J,Qi J,Gao GFdoi
10.1016/j.celrep.2013.01.025subject
Has Abstractpub_date
2013-03-28 00:00:00pages
769-78issue
3issn
2211-1247pii
S2211-1247(13)00032-6journal_volume
3pub_type
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