Evidence map›Paper›PMID 36457099›Full record

ArticleVirology journal2022

Identification of a neutralizing linear epitope within the VP1 protein of coxsackievirus A10.

Hanyu Zhu, Xin Liu, Yue Wu, Yunyi He, Huanying Zheng, Hongbo Liu, Qiliang Liu

Open access · goldAbstract read
In one paragraph

Article in Virology journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.5field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 10 citations in OpenAlex.

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  5. Experimental animal models for development of human enterovirus vaccine.Clinical and experimental vaccine research · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Hanyu Zhu *College of Intelligent Medicine and Biotechnology, Guilin Medical University, Guilin, Guangxi, China.
Xin Liu *College of Intelligent Medicine and Biotechnology, Guilin Medical University, Guilin, Guangxi, China.
Yue Wu *Department of Laboratory Medicine, The Second Affiliated Hospital of Guilin Medical University, Guilin, Guangxi, China.
Yunyi HeDepartment of Laboratory Medicine, The Second Affiliated Hospital of Guilin Medical University, Guilin, Guangxi, China.
Huanying ZhengGuangdong Provincial Institute of Public Health, Guangdong Provincial Center for Disease Control and Prevention, Guangzhou, Guangdong, China.
Hongbo LiuDepartment of Laboratory Medicine, The Second Affiliated Hospital of Guilin Medical University, Guilin, Guangxi, China. hbliu@glmc.edu.cn.
Qiliang LiuCollege of Intelligent Medicine and Biotechnology, Guilin Medical University, Guilin, Guangxi, China. aqua02@126.com.
Guilin Medical University · CNGuangdong Provincial Center for Disease Control and Prevention · CNHealth Commission of Anhui Province · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCoxsackievirus A10 (CV-A10) is a leading cause of hand, foot, and mouth disease (HFMD). It is necessary to identify neutralizing epitopes to investigate and develop an epitope-based vaccine against CV-A10. The viral protein VP1 is the immunodominant capsid protein and contains the critical neutralizing epitope. However, neutralizing epitopes within VP1 protein of CV-A10 have not been well characterized.

methodsBioinformatics techniques were applied to predict linear epitopes on the CV-A10 VP1 protein. The advanced structural features of epitopes were analyzed by three-dimensional (3D) modeling. The anticipated epitope peptides were synthesized and used to immunize mice as antigens. ELISA and micro-neutralization assay were used to determine the specific IgG antibody and neutralizing antibody titers. The protective efficacy of the epitope peptides in vivo was evaluated using a passive immunization/challenge assay.

resultsThree linear epitopes (EP3, EP4, and EP5) were predicted on CV-A10 VP1, all spatially exposed on the capsid surface, and exhibited adequate immunogenicity. However, only EP4, corresponding to residues 162-176 of VP1, demonstrated potent neutralization against CV-A10. To determine the neutralizing capacity of EP4 further, EP4 double-peptide was synthesized and injected into mice. The mean neutralizing antibody titer of the anti-EP4 double-peptide sera was 1:50.79, which provided 40% protection against lethal infection with CV-A10 in neonatal mice. In addition, sequence and advanced structural analysis revealed that EP4 was highly conserved among representative strains of CV-A10 and localized in the EF loop region of VP1, like EV-A71 SP55 or CV-A16 PEP55.

conclusionsThese data demonstrate that EP4 is a specific linear neutralizing epitope on CV-A10 VP1. Its protective efficacy can be enhanced by increasing its copy number, which will be the foundation for developing a CV-A10 epitope-based vaccine.

Indexed as

Capsid ProteinsComputational BiologyEnterovirusAnimalsAntibodies, NeutralizingEpitopesMiceAntibodies, NeutralizingCapsid ProteinsEpitopesBioinformaticsCoxsackievirus A10EpitopeNeutralization

Identifiers

PMID36457099
PMCPMC9714398
OpenAlexW4310494125

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.