tetano
Editor, Senior Moderator
Biochemistry. 2014 Jan 16. [Epub ahead of print]
Structural Insights into Membrane-fusion Mechanism Mediated by Influenza Virus Hemagglutinin.
Ni FY, Chen X, Shen J, Wang Q.
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 at post-fusion state. Together with a large number of previously determined pre-fusion structures of influenza A and B virus HA and a post-fusion 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.
PMID:
24433110
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24433110
Structural Insights into Membrane-fusion Mechanism Mediated by Influenza Virus Hemagglutinin.
Ni FY, Chen X, Shen J, Wang Q.
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 at post-fusion state. Together with a large number of previously determined pre-fusion structures of influenza A and B virus HA and a post-fusion 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.
PMID:
24433110
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24433110