Evidence map›Paper›PMID 29765376›Full record

ArticleFrontiers in immunology2018

Immunization With Fc-Based Recombinant Epstein-Barr Virus gp350 Elicits Potent Neutralizing Humoral Immune Response in a BALB/c Mice Model.

Bingchun Zhao, Xiao Zhang, Claude Krummenacher, Shuo Song, Ling Gao, Haojiong Zhang, Miao Xu, Lin Feng, Qisheng Feng, Musheng Zeng and 2 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

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  19. Vaccination against the Epstein-Barr virus.Cellular and molecular life sciences : CMLS · 2020
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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

12 authors at 5 institutions in 2 countries.

Bingchun ZhaoGuangdong Key Laboratory of Nasopharyngeal Carcinoma Diagnosis and Therapy, State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Department of Experimental Research, Sun Yat-Sen University Cancer Center, Guangzhou, China.
Xiao ZhangGuangdong Key Laboratory of Nasopharyngeal Carcinoma Diagnosis and Therapy, State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Department of Experimental Research, Sun Yat-Sen University Cancer Center, Guangzhou, China.
Claude KrummenacherDepartment of Biological Sciences, Rowan University, Glassboro, NJ, United States.
Shuo SongState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China.
Ling GaoGuangdong Key Laboratory of Nasopharyngeal Carcinoma Diagnosis and Therapy, State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Department of Experimental Research, Sun Yat-Sen University Cancer Center, Guangzhou, China.
Haojiong ZhangGuangdong Key Laboratory of Nasopharyngeal Carcinoma Diagnosis and Therapy, State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Department of Experimental Research, Sun Yat-Sen University Cancer Center, Guangzhou, China.
Miao XuGuangdong Key Laboratory of Nasopharyngeal Carcinoma Diagnosis and Therapy, State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Department of Experimental Research, Sun Yat-Sen University Cancer Center, Guangzhou, China.
Lin FengGuangdong Key Laboratory of Nasopharyngeal Carcinoma Diagnosis and Therapy, State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Department of Experimental Research, Sun Yat-Sen University Cancer Center, Guangzhou, China.
Qisheng FengGuangdong Key Laboratory of Nasopharyngeal Carcinoma Diagnosis and Therapy, State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Department of Experimental Research, Sun Yat-Sen University Cancer Center, Guangzhou, China.
Musheng ZengGuangdong Key Laboratory of Nasopharyngeal Carcinoma Diagnosis and Therapy, State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Department of Experimental Research, Sun Yat-Sen University Cancer Center, Guangzhou, China.
Yuting XuGuiyang City National High School, Guiyang, China.
Yixin ZengGuangdong Key Laboratory of Nasopharyngeal Carcinoma Diagnosis and Therapy, State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Department of Experimental Research, Sun Yat-Sen University Cancer Center, Guangzhou, China.
Sun Yat-sen University Cancer Center · CNSun Yat-sen University · CNGuiyang University · CNRowan University · USXiamen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epstein-Barr virus (EBV) was the first human virus proved to be closely associated with tumor development, such as lymphoma, nasopharyngeal carcinoma, and EBV-associated gastric carcinoma. Despite many efforts to develop prophylactic vaccines against EBV infection and diseases, no candidates have succeeded in effectively blocking EBV infection in clinical trials. Previous investigations showed that EBV gp350 plays a pivotal role in the infection of B-lymphocytes. Nevertheless, using monomeric gp350 proteins as antigens has not been effective in preventing infection. Multimeric forms of the antigen are more potently immunogenic than monomers; however, the multimerization elements used in previous constructs are not approved for human clinical trials. To prepare a much-needed EBV prophylactic vaccine that is potent, safe, and applicable, we constructed an Fc-based form of gp350 to serve as a dimeric antigen. Here, we show that the Fc-based gp350 antigen exhibits dramatically enhanced immunogenicity compared with wild-type gp350 protein. The complete or partial gp350 ectodomain was fused with the mouse IgG2a Fc domain. Fusion with the Fc domain did not impair gp350 folding, binding to a conformation-dependent neutralizing antibody (nAb) and binding to its receptor by enzyme-linked immunosorbent assay and surface plasmon resonance. Specific antibody titers against gp350 were notably enhanced by immunization with gp350-Fc dimers compared with gp350 monomers. Furthermore, immunization with gp350-Fc fusion proteins elicited potent nAbs against EBV. Our data strongly suggest that an EBV gp350 vaccine based on Fc fusion proteins may be an efficient candidate to prevent EBV infection in clinical applications.

Indexed as

Recombinant Fusion ProteinsAdjuvants, ImmunologicAnimalsAntibodies, NeutralizingAntibodies, ViralEpstein-Barr Virus InfectionsHerpesvirus 4, HumanHumansImmunity, HumoralImmunizationImmunoglobulin AImmunoglobulin Fc FragmentsImmunoglobulin GKineticsMiceMice, Inbred BALB CAdjuvants, ImmunologicAntibodies, NeutralizingAntibodies, ViralImmunoglobulin AImmunoglobulin Fc FragmentsImmunoglobulin GRecombinant Fusion ProteinsViral Proteinsenvelope proteinEpstein–Barr virusFc-based vaccinegp350intranasal immunizationneutralizing antibody

Identifiers

PMID29765376
PMCPMC5938345
OpenAlexW2800496519

What OpenQuestion holds

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Registered trials

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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.