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Design and Structure of an Engineered Disulfide-Stabilized Influenza Hemagglutinin Trimer

tetano

Editor, Senior Moderator
J Virol. 2015 Apr 29. pii: JVI.00808-15. [Epub ahead of print]
[h=1]Design and Structure of an Engineered Disulfide-Stabilized Influenza Hemagglutinin Trimer.[/h] Lee PS[SUP]1[/SUP], Zhu X[SUP]2[/SUP], Yu W[SUP]2[/SUP], Wilson IA[SUP]3[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] We engineered a disulfide-stabilized influenza hemagglutinin (HA) trimer, termed HA[SUB]3[/SUB]-SS, by introducing cysteine residues in the HA stem to covalently bridge the three protomers. HA[SUB]3[/SUB]-SS has increased thermostability compared to wild-type HA and binding of head- and stem-targeted antibodies is preserved; only minor structural changes are found in the vicinity of the additional disulfide. This platform has been applied to H1 and H3 HAs and provides prospects for design of intact, stabilized influenza HA immunogens.
Copyright ? 2015, American Society for Microbiology. All Rights Reserved.


PMID: 25926650 [PubMed - as supplied by publisher]
 
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