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TitleAntigen spacing on protein nanoparticles influences antibody responses to vaccination.
Journal, issue, pagesCell Rep, Vol. 42, Issue 12, Page 113552, Year 2023
Publish dateDec 13, 2023
AuthorsDaniel Ellis / Annie Dosey / Seyhan Boyoglu-Barnum / Young-Jun Park / Rebecca Gillespie / Hubza Syeda / Geoffrey B Hutchinson / Yaroslav Tsybovsky / Michael Murphy / Deleah Pettie / Nick Matheson / Sidney Chan / George Ueda / Jorge A Fallas / Lauren Carter / Barney S Graham / David Veesler / Masaru Kanekiyo / Neil P King /
PubMed AbstractImmunogen design approaches aim to control the specificity and quality of antibody responses elicited by next-generation vaccines. Here, we use computational protein design to generate a nanoparticle ...Immunogen design approaches aim to control the specificity and quality of antibody responses elicited by next-generation vaccines. Here, we use computational protein design to generate a nanoparticle vaccine platform based on the receptor-binding domain (RBD) of influenza hemagglutinin (HA) that enables precise control of antigen conformation and spacing. HA RBDs are presented as either monomers or native-like closed trimers that are connected to the underlying nanoparticle by a rigid linker that is modularly extended to precisely control antigen spacing. Nanoparticle immunogens with decreased spacing between trimeric RBDs elicit antibodies with improved hemagglutination inhibition and neutralization potency as well as binding breadth across diverse H1 HAs. Our "trihead" nanoparticle immunogen platform provides insights into anti-HA immunity, establishes antigen spacing as an important parameter in structure-based vaccine design, and embodies several design features that could be used in next-generation vaccines against influenza and other viruses.
External linksCell Rep / PubMed:38096058 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 6.8 Å
Structure data

EMDB-42481: I53_dn5 nanoparticle displaying the trimeric HA heads with heptad domain, TH-1heptad-I53_dn5
Method: EM (single particle) / Resolution: 4.1 Å

42482

8ur5

EMDB-42482, PDB-8ur5:
I53_dn5 nanoparticle displaying the trimeric HA heads with heptad domain, TH-1heptad-I53_dn5 (local refinement of TH-1heptad)
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-42483: I53_dn5 nanoparticle displaying the trimeric HA heads with heptad domain, TH-2heptad-I53_dn5
Method: EM (single particle) / Resolution: 6.8 Å

EMDB-42485: I53_dn5 nanoparticle displaying the trimeric HA heads with heptad domain, TH-6heptad-I53_dn5
Method: EM (single particle) / Resolution: 4.0 Å

42486

8ur7

EMDB-42486, PDB-8ur7:
I53_dn5 nanoparticle displaying the trimeric HA heads with heptad domain, TH-6heptad-I53_dn5 (local refinement of TH-6heptad)
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • synthetic construct (others)
  • influenza a virus
KeywordsVIRAL PROTEIN / Influenza virus / Hemagglutinin nanoparticle vaccine / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID

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