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TitleNeutralizing antibodies elicited in nonhuman primates by an enterovirus D68 virus-like particle vaccine target receptor binding sites.
Journal, issue, pagesSci Transl Med, Vol. 18, Issue 852, Page eaec5446, Year 2026
Publish dateJun 3, 2026
AuthorsDaniel L Moss / Jiaxuan Cheng / Peter W Krug / Alden C Paine / Brian E Fisher / Amy R Henry / Jesmine Roberts-Torres / Timothy S Johnston / Sarah C Smith / Sergei Pletnev / Haotian Lei / Nicholas C Morano / Theodore C Pierson / Lawrence Shapiro / Tongqing Zhou / Peter D Kwong / Daniel C Douek / Masaru Kanekiyo / Tracy J Ruckwardt /
PubMed AbstractEnterovirus D68 (EV-D68) is a picornavirus that causes biennial outbreaks of respiratory disease in young children that can progress to rare but severe complications, including acute flaccid myelitis ...Enterovirus D68 (EV-D68) is a picornavirus that causes biennial outbreaks of respiratory disease in young children that can progress to rare but severe complications, including acute flaccid myelitis (AFM). EV-D68 virus-like particles (VLPs) elicit potent neutralizing antibodies that are protective in animal models. Here, we report the isolation and characterization of monoclonal antibodies elicited by EV-D68 VLPs in nonhuman primates (NHPs). We identified five potently neutralizing mAbs targeting overlapping epitopes near the capsid fivefold axis of symmetry formed by pentamers of viral protein 1. Cryo-electron microscopy structures of mAbs 1E11 and 5H03 in complex with VLP revealed epitopes on the capsid that bridge the sialic acid binding site and the proteinaceous entry receptor major facilitator superfamily domain-containing protein 6 binding site. We further characterized the mechanisms by which these mAbs neutralize EV-D68 and found that mAbs can disrupt multiple steps in the EV-D68 life cycle, including promoting premature uncoating. Antibodies elicited by VLP immunization of NHP protected as well as a best-in-class human mAb in a mouse challenge model, although single-amino acid mutations in the capsid enabled viral escape. Our results demonstrate that EV-D68 VLP-elicited mAbs target major viral sites of vulnerability, provide insight into their mechanisms of neutralization, and reinforce the potential for VLP-based vaccines as a countermeasure for EV-D68.
External linksSci Transl Med / PubMed:42234771
MethodsEM (single particle)
Resolution2.63 - 2.83 Å
Structure data

75818

11lt

EMDB-75818, PDB-11lt:
Cryo-EM structure of EV-D68 B3 VLP bound by neutralizing antibody 1E11
Method: EM (single particle) / Resolution: 2.63 Å

75894

11ov

EMDB-75894, PDB-11ov:
Cryo-EM structure of EV-D68 B3 VLP bound by neutralizing antibody 5H03
Method: EM (single particle) / Resolution: 2.83 Å

Source
  • human enterovirus d68
  • macaca mulatta (Rhesus monkey)
KeywordsVIRUS LIKE PARTICLE / EV-D68 / B3 subclade / Virus-like particle vaccine / 1E11 neutralizing antibody / 5H03 neutralizing antibody

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