Why the study?
Echovirus 3 causes severe diseases in infants, but the structural basis for its specificities and immunological characteristics was incompletely understood.
The structural characterization of the highly immunogenic C-terminus of VP1 in Echovirus 3 provides new strategies for vaccine development against human enterovirus B.
Structural details of E3-antibody binding may guide future immunotherapies in infants; leaves open clinical translation pending functional studies.
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.
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Qi et al. (2022) studied this question.
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