Abstract：
:Membrane fusion is involved in many fundamental cellular processes and entry of enveloped viruses into host cells. Influenza type A virus HA has long served as a paradigm for mechanistic studies of protein-mediated membrane fusion via large-scale structural rearrangements induced by acidic pH. Here we report the newly determined crystal structure of influenza B virus HA2 in the postfusion state. Together with a large number of previously determined prefusion structures of influenza A and B virus HA and a postfusion structure of influenza A/H3N2 HA2, we identified conserved features that are shared between influenza A and B virus HA in the conformational transition and documented substantial differences that likely influence the detailed mechanisms of this process. Further studies are needed to dissect the effects of these and other structural differences in HA conformational changes and influenza pathogenicity and transmission, which may ultimately expedite the discovery of novel anti-influenza fusion inhibitors.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Ni F,Chen X,Shen J,Wang Qdoi
10.1021/bi401525hsubject
Has Abstractpub_date
2014-02-11 00:00:00pages
846-54issue
5eissn
0006-2960issn
1520-4995journal_volume
53pub_type
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