8UR5

I53_dn5 nanoparticle displaying the trimeric HA heads with heptad domain, TH-1heptad-I53_dn5 (local refinement of TH-1heptad)

8UR5 の概要

• エントリーDOI: 10.2210/pdb8ur5/pdb
• EMDBエントリー: 42482
• 分子名称: Trimer head HA,Hemagglutinin HA1 chain, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: influenza virus, hemagglutinin nanoparticle vaccine, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein
• 由来する生物種: synthetic construct; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 135415.11

構造登録者

Park, Y.J.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2023-10-25, 公開日: 2023-12-27, 最終更新日: 2024-10-16)

主引用文献

Ellis, D.,Dosey, A.,Boyoglu-Barnum, S.,Park, Y.J.,Gillespie, R.,Syeda, H.,Hutchinson, G.B.,Tsybovsky, Y.,Murphy, M.,Pettie, D.,Matheson, N.,Chan, S.,Ueda, G.,Fallas, J.A.,Carter, L.,Graham, B.S.,Veesler, D.,Kanekiyo, M.,King, N.P.
Antigen spacing on protein nanoparticles influences antibody responses to vaccination.
Cell Rep, 42:113552-113552, 2023

PubMed Abstract: 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.

PubMed: 38096058
DOI: 10.1016/j.celrep.2023.113552

実験手法

ELECTRON MICROSCOPY (3.7 Å)