Evidence map›Paper›PMID 36805409›Full record

ArticleVirus research2023

Identification of specific and shared epitopes at the extreme N-terminal VP1 of Coxsackievirus A4, A2 and A5 by monoclonal antibodies.

Yu-Xuan Tian, Wei-Ping Jin, Zhen-Ni Wei, Shi-Yun Lv, Meng-Jun Wang, Sheng-Li Meng, Jing Guo, Ze-Jun Wang, Shuo Shen

Open access · goldAbstract read
In one paragraph

Article in Virus research, 2023. 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, 7 citations in OpenAlex.

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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

9 authors at 2 institutions in 2 countries.

Yu-Xuan TianWuhan Institute of Biological Products Co. Ltd., No.1 Huangjin Industrial Park Road, Jiangxia District, Wuhan 430207, China.
Wei-Ping JinWuhan Institute of Biological Products Co. Ltd., No.1 Huangjin Industrial Park Road, Jiangxia District, Wuhan 430207, China.
Zhen-Ni WeiWuhan Institute of Biological Products Co. Ltd., No.1 Huangjin Industrial Park Road, Jiangxia District, Wuhan 430207, China.
Shi-Yun LvWuhan Institute of Biological Products Co. Ltd., No.1 Huangjin Industrial Park Road, Jiangxia District, Wuhan 430207, China.
Meng-Jun WangWuhan Institute of Biological Products Co. Ltd., No.1 Huangjin Industrial Park Road, Jiangxia District, Wuhan 430207, China.
Sheng-Li MengWuhan Institute of Biological Products Co. Ltd., No.1 Huangjin Industrial Park Road, Jiangxia District, Wuhan 430207, China.
Jing GuoWuhan Institute of Biological Products Co. Ltd., No.1 Huangjin Industrial Park Road, Jiangxia District, Wuhan 430207, China.
Ze-Jun WangWuhan Institute of Biological Products Co. Ltd., No.1 Huangjin Industrial Park Road, Jiangxia District, Wuhan 430207, China.
Shuo ShenWuhan Institute of Biological Products Co. Ltd., No.1 Huangjin Industrial Park Road, Jiangxia District, Wuhan 430207, China. Electronic address: shenshuo0227@qq.com.
Wuhan Institute of Bioengineering · CNAjinomoto (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hand, foot and mouth disease (HFMD) is caused by a variety of serotypes in species A of the Enterovirus genus, including recently re-emerged Coxsackievirus A2 (CV-A2), CV-A4 and CV-A5. For development of diagnostic reagents, for surveillance, and the development of multivalent vaccines against HFMD, the antigenicity of HFMD-associated enteroviruses warrants investigation. The purified virions of CV-A4 were inoculated into Balb/c mice and hybridomas were obtained secreting monoclonal antibodies (mAbs) directed against CV-A4 and cross-reacting with other closely related species A enteroviruses. The mAbs were characterized by ELISA, Western blotting and in vitro neutralizing assays. The majority of mAbs was non-neutralizing, with only 2% of the mAbs neutralizing CV-A4 specifically. Most of mAbs bound to linear VP1 epitopes of CV-A4. Interestingly, four types of mAbs were obtained which bound specifically to CV-A4 or were broadly to CV-A4/-A2, CV-A4/-A5 and CV-A4/-A2/-A5, respectively. Mapping with overlapping or single-amino-acid mutant peptides revealed that the four types of mAbs all bound to the first 15 amino acids at the N-terminus of the VP1. This region of picornaviruses is functionally important as it is involved in uncoating and releasing of viral RNA into the cytosol. The binding footprints of four type mAbs are composed of conserved and variable residues and are different from each other. The newly discovered broadly cross-reactive mAbs reflect the high homology of CV-A4/ CV-A2/CV-A5. The results also demonstrate that it is possible and beneficial to develop the diagnostic reagents to detect rapidly the main pathogens of enteroviruses associated with HFMD cause by CV-A4/CV-A2/CV-A5.

Indexed as

EnterovirusEnterovirus A, HumanEnterovirus InfectionsHand, Foot and Mouth DiseaseAnimalsAntibodies, MonoclonalAntigens, ViralChinaEpitopesMiceAntibodies, MonoclonalAntigens, ViralEpitopesBroadly binding activityCoxsackievirus A2/A4/A5EpitopesMonoclonal antibodies

Identifiers

PMID36805409
PMCPMC10194160
OpenAlexW4321478742

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.