tetano
Editor, Senior Moderator
Cold Spring Harb Perspect Med. 2019 Dec 23. pii: a038778. doi: 10.1101/cshperspect.a038778. [Epub ahead of print] [h=1]Influenza Hemagglutinin Structures and Antibody Recognition.[/h]
Wu NC[SUP]1[/SUP], Wilson IA[SUP]1,[/SUP][SUP]2[/SUP].
[h=3]Author information[/h] 1 Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037, USA. 2 The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
[h=3]Abstract[/h] Hemagglutinin (HA) is most abundant glycoprotein on the influenza virus surface. Influenza HA promotes viral entry by engaging the receptor and mediating virus-host membrane fusion. At the same time, HA is the major antigen of the influenza virus. HA antigenic shift can result in pandemics, whereas antigenic drift allows human circulating strains to escape herd immunity. Most antibody responses against HA are strain-specific. However, antibodies that have neutralizing activities against multiple strains or even subtypes have now been discovered and characterized. These broadly neutralizing antibodies (bnAbs) target conserved regions on HA, such as the receptor-binding site and the stem domain. Structural studies of such bnAbs have provided important insight into universal influenza vaccine and therapeutic design. This review discusses the HA functions as well as HA-antibody interactions from a structural perspective.
Copyright ? 2019 Cold Spring Harbor Laboratory Press; all rights reserved.
PMID: 31871236 DOI: 10.1101/cshperspect.a038778
Wu NC[SUP]1[/SUP], Wilson IA[SUP]1,[/SUP][SUP]2[/SUP].
[h=3]Author information[/h] 1 Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037, USA. 2 The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
[h=3]Abstract[/h] Hemagglutinin (HA) is most abundant glycoprotein on the influenza virus surface. Influenza HA promotes viral entry by engaging the receptor and mediating virus-host membrane fusion. At the same time, HA is the major antigen of the influenza virus. HA antigenic shift can result in pandemics, whereas antigenic drift allows human circulating strains to escape herd immunity. Most antibody responses against HA are strain-specific. However, antibodies that have neutralizing activities against multiple strains or even subtypes have now been discovered and characterized. These broadly neutralizing antibodies (bnAbs) target conserved regions on HA, such as the receptor-binding site and the stem domain. Structural studies of such bnAbs have provided important insight into universal influenza vaccine and therapeutic design. This review discusses the HA functions as well as HA-antibody interactions from a structural perspective.
Copyright ? 2019 Cold Spring Harbor Laboratory Press; all rights reserved.
PMID: 31871236 DOI: 10.1101/cshperspect.a038778