tetano
Editor, Senior Moderator
J Mol Biol. 2017 May 12. pii: S0022-2836(17)30226-7. doi: 10.1016/j.jmb.2017.05.011. [Epub ahead of print]
[h=1]CryoEM structure of an influenza virus receptor-binding site antibody-antigen interface.[/h] Liu Y[SUP]1[/SUP], Pan J[SUP]2[/SUP], Jenni S[SUP]3[/SUP], Raymond DD[SUP]2[/SUP], Caradonna T[SUP]3[/SUP], Do KT[SUP]2[/SUP], Schmidt AG[SUP]4[/SUP], Harrison SC[SUP]5[/SUP], Grigorieff N[SUP]6[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Structure-based vaccine design depends on extensive structural analyses of antigen-antibody complexes. Single-particle electron cryomicroscopy (cryoEM) can circumvent some of the problems of x-ray crystallography as a pipeline for obtaining the required structures. We have examined the potential of single-particle cryoEM for determining the structure of influenza-virus hemagglutinin (HA):single-chain Fv (scFv) complexes, by studying a complex we failed to crystallize in pursuing an extended project of the human immune response to influenza vaccines. The result shows that a combination of cryoEM and molecular modeling can yield details of the antigen:antibody interface, although small variation in the twist of the rod-like HA trimer limited the overall resolution to about 4.5?. Comparison of principal 3D classes suggests ways to modify the HA trimer to overcome this limitation. A closely related antibody from the same donor did yield crystals when bound with the same HA, giving us an independent validation of the cryoEM results The two structures also augment our understanding of receptor-binding site recognition by antibodies that neutralize a wide range of influenza-virus variants.
Copyright ? 2017. Published by Elsevier Ltd.
[h=4]KEYWORDS:[/h] antibody binding; electron cryomicroscopy (cryoEM); influenza virus hemagglutinin; x-ray crystallography
PMID: 28506635 DOI: 10.1016/j.jmb.2017.05.011
[h=1]CryoEM structure of an influenza virus receptor-binding site antibody-antigen interface.[/h] Liu Y[SUP]1[/SUP], Pan J[SUP]2[/SUP], Jenni S[SUP]3[/SUP], Raymond DD[SUP]2[/SUP], Caradonna T[SUP]3[/SUP], Do KT[SUP]2[/SUP], Schmidt AG[SUP]4[/SUP], Harrison SC[SUP]5[/SUP], Grigorieff N[SUP]6[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Structure-based vaccine design depends on extensive structural analyses of antigen-antibody complexes. Single-particle electron cryomicroscopy (cryoEM) can circumvent some of the problems of x-ray crystallography as a pipeline for obtaining the required structures. We have examined the potential of single-particle cryoEM for determining the structure of influenza-virus hemagglutinin (HA):single-chain Fv (scFv) complexes, by studying a complex we failed to crystallize in pursuing an extended project of the human immune response to influenza vaccines. The result shows that a combination of cryoEM and molecular modeling can yield details of the antigen:antibody interface, although small variation in the twist of the rod-like HA trimer limited the overall resolution to about 4.5?. Comparison of principal 3D classes suggests ways to modify the HA trimer to overcome this limitation. A closely related antibody from the same donor did yield crystals when bound with the same HA, giving us an independent validation of the cryoEM results The two structures also augment our understanding of receptor-binding site recognition by antibodies that neutralize a wide range of influenza-virus variants.
Copyright ? 2017. Published by Elsevier Ltd.
[h=4]KEYWORDS:[/h] antibody binding; electron cryomicroscopy (cryoEM); influenza virus hemagglutinin; x-ray crystallography
PMID: 28506635 DOI: 10.1016/j.jmb.2017.05.011