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TitleBroadly therapeutic antibody provides cross-serotype protection against enteroviruses via Fc effector functions and by mimicking SCARB2.
Journal, issue, pagesNat Microbiol, Vol. 9, Issue 11, Page 2939-2953, Year 2024
Publish dateOct 18, 2024
AuthorsRui Zhu / Yuanyuan Wu / Yang Huang / Yanan Jiang / Yichao Jiang / Dongqing Zhang / Hui Sun / Zhenhong Zhou / Lizhi Zhou / Shihan Weng / Hao Chen / Xiaoqing Chen / Wenjing Ning / Yuxiang Zou / Maozhou He / Hongwei Yang / Weixi Deng / Yu Li / Zhenqin Chen / Xiangzhong Ye / Jinle Han / Zhichao Yin / Huan Zhao / Che Liu / Yuqiong Que / Mujin Fang / Hai Yu / Jun Zhang / Wenxin Luo / Shaowei Li / Qingbing Zheng / Longfa Xu / Ningshao Xia / Tong Cheng /
PubMed AbstractEnteroviruses contain multiple serotypes and can cause severe neurological complications. The intricate life cycle of enteroviruses involving dynamic virus-receptor interaction hampers the ...Enteroviruses contain multiple serotypes and can cause severe neurological complications. The intricate life cycle of enteroviruses involving dynamic virus-receptor interaction hampers the development of broad therapeutics and vaccines. Here, using function-based screening, we identify a broadly therapeutic antibody h1A6.2 that potently protects mice in lethal models of infection with both enterovirus A71 and coxsackievirus A16 through multiple mechanisms, including inhibition of the virion-SCARB2 interactions and monocyte/macrophage-dependent Fc effector functions. h1A6.2 mitigates inflammation and improves intramuscular mechanics, which are associated with diminished innate immune signalling and preserved tissue repair. Moreover, cryogenic electron microscopy structures delineate an adaptive binding of h1A6.2 to the flexible and dynamic nature of the VP2 EF loop with a binding angle mimicking the SCARB2 receptor. The coordinated binding mode results in efficient binding of h1A6.2 to all viral particle types and facilitates broad neutralization of enterovirus, therefore informing a promising target for the structure-guided design of pan-enterovirus vaccine.
External linksNat Microbiol / PubMed:39424982
MethodsEM (single particle)
Resolution2.89 - 3.82 Å
Structure data

38165

8x95

EMDB-38165, PDB-8x95:
Cryo-EM structure of enterovirus A71 mature virion in complex with Fab h1A6.2
Method: EM (single particle) / Resolution: 3.52 Å

38166

8x96

EMDB-38166, PDB-8x96:
Cryo-EM structure of enterovirus A71 A-particle in complex with Fab h1A6.2
Method: EM (single particle) / Resolution: 2.89 Å

38167

8x97

EMDB-38167, PDB-8x97:
Cryo-EM structure of enterovirus A71 empty particle in complex with Fab h1A6.2
Method: EM (single particle) / Resolution: 2.98 Å

38168

8x98

EMDB-38168, PDB-8x98:
Cryo-EM structure of coxsackievirus A16 mature virion in complex with Fab h1A6.2
Method: EM (single particle) / Resolution: 3.69 Å

38169

8x99

EMDB-38169, PDB-8x99:
Cryo-EM structure of coxsackievirus A16 A-particle in complex with Fab h1A6.2
Method: EM (single particle) / Resolution: 3.38 Å

38170

8x9a

EMDB-38170, PDB-8x9a:
Cryo-EM structure of coxsackievirus A16 empty particle in complex with Fab h1A6.2
Method: EM (single particle) / Resolution: 3.36 Å

38171

8x9b

EMDB-38171, PDB-8x9b:
Cryo-EM structure of coxsackievirus A16 empty particle in complex with Fab h1A6.2 (local refinement)
Method: EM (single particle) / Resolution: 3.82 Å

39570

8ytb

EMDB-39570, PDB-8ytb:
Cryo-EM structure of enterovirus A71 empty particle
Method: EM (single particle) / Resolution: 2.96 Å

39572

8ytj

EMDB-39572, PDB-8ytj:
Cryo-EM structure of enterovirus A71 mature virion
Method: EM (single particle) / Resolution: 3.07 Å

Chemicals

ChemComp-SPH:
SPHINGOSINE

Source
  • Mus (mice)
  • enterovirus a71
  • coxsackievirus a16
  • mus musculus (house mouse)
KeywordsVIRUS / ENTEROVIRUS A71 / Cryo-EM STRUCTURE / Cryo-EM / coxsackievirus A16 / VIRAL PROTEIN

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