Structural Basis for the Immunogenicity of the C-Terminus of VP1 of Echovirus 3 Revealed by the Binding of a Neutralizing Antibody

Viruses. 2022 Oct 22;14(11):2322. doi: 10.3390/v14112322.

Abstract

Echovirus 3 (E3), a serotype of human enterovirus B (HEV-B), causes severe diseases in infants. Here, we determined the structures of E3 with a monoclonal antibody (MAb) 6D10 by cryo-EM to comprehensively understand the specificities and the immunological characteristic of this serotype. The solved cryo-EM structures of the F-, A-, and E-particles of E3 bound with 6D10 revealed the structural features of the virus-antibody interface. Importantly, the structures of E-particles bound with 6D10 revealed for the first time the nature of the C-terminus of VP1 for HEV-Bs at the structural level. The highly immunogenic nature of this region in the E-particles provides new strategies for vaccine development for HEV-Bs.

Keywords: C-terminus of VP1; cryo-EM single particle analysis; echovirus 3; monoclonal antibody (MAb); structures; vaccine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal
  • Antibodies, Neutralizing*
  • Antibodies, Viral
  • Enterovirus B, Human*
  • Humans
  • Serogroup

Substances

  • Antibodies, Neutralizing
  • Antibodies, Monoclonal
  • Antibodies, Viral

Grants and funding

This work was supported by funding from the Beijing Natural Science Foundation–Haidian Primitive Innovation Joint Fund (L192008), the National Science Foundation of China (31800145), the Ministry of Science and Technology of China (CPNL2022A-03-03, CPNL-1233, and EKPG21-09), the National Key R&D Program (2020YFA0707500, 2018YFA0900801, and 2021YFA1301400), and the National Natural Science Foundation of China (31872730 and 32070947). Ling Zhu was supported by the Youth Innovation Promotion Association at the Chinese Academy of Sciences (2019098).