EMD-9601
The structure of CVA10 virus procapsid particle
EMD-9601
Single-particle4.0 Å
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Map released: 21/11/2018
Last modified: 29/05/2024
Sample Organism:
Coxsackievirus A10
Sample: CVA10 virus procapsid particle
Fitted models: 6acw (Avg. Q-score: 0.476)
Deposition Authors: Zhu R
,
Xu LF
Sample: CVA10 virus procapsid particle
Fitted models: 6acw (Avg. Q-score: 0.476)
Deposition Authors: Zhu R
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Discovery and structural characterization of a therapeutic antibody against coxsackievirus A10.
Zhu R
,
Xu L
,
Zheng Q
,
Cui Y
,
Li S
,
He M,
Yin Z
,
Liu D,
Li S
,
Li Z,
Chen Z,
Yu H
,
Que Y,
Liu C,
Kong Z,
Zhang J,
Baker TS
,
Yan X
,
Hong Zhou Z
,
Cheng T
,
Xia N
(2018) Sci Adv , 4 , eaat7459 - eaat7459
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(2018) Sci Adv , 4 , eaat7459 - eaat7459
Abstract:
Coxsackievirus A10 (CVA10) recently emerged as a major pathogen of hand, foot, and mouth disease and herpangina in children worldwide, and lack of a vaccine or a cure against CVA10 infections has made therapeutic antibody identification a public health priority. By targeting a local isolate, CVA10-FJ-01, we obtained a potent antibody, 2G8, against all three capsid forms of CVA10. We show that 2G8 exhibited both 100% preventive and 100% therapeutic efficacy against CVA10 infection in mice. Comparisons of the near-atomic cryo-electron microscopy structures of the three forms of CVA10 capsid and their complexes with 2G8 Fab reveal that a single Fab binds a border region across the three capsid proteins (VP1 to VP3) and explain 2G8's remarkable cross-reactivities against all three capsid forms. The atomic structures of this first neutralizing antibody of CVA10 should inform strategies for designing vaccines and therapeutics against CVA10 infections.
Coxsackievirus A10 (CVA10) recently emerged as a major pathogen of hand, foot, and mouth disease and herpangina in children worldwide, and lack of a vaccine or a cure against CVA10 infections has made therapeutic antibody identification a public health priority. By targeting a local isolate, CVA10-FJ-01, we obtained a potent antibody, 2G8, against all three capsid forms of CVA10. We show that 2G8 exhibited both 100% preventive and 100% therapeutic efficacy against CVA10 infection in mice. Comparisons of the near-atomic cryo-electron microscopy structures of the three forms of CVA10 capsid and their complexes with 2G8 Fab reveal that a single Fab binds a border region across the three capsid proteins (VP1 to VP3) and explain 2G8's remarkable cross-reactivities against all three capsid forms. The atomic structures of this first neutralizing antibody of CVA10 should inform strategies for designing vaccines and therapeutics against CVA10 infections.