Evidence map›Paper›PMID 41703287›Full record

ArticleCommunications biology2026

Immunogenicity assessment and epitope mapping of the ASFV proteome by profiling serum antibodies with ASFV antigen phage libraries.

Lerong Ma, Zhen Weng, Yuanzhu Zhang, Zhi Cao, Xingjun Ke, Ruize Sun, Yin Xie, Mengjie Lian, Lin Yang, Hongming Yuan and 4 more

Abstract read
In one paragraph

Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Article
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

14 authors.

Lerong Ma *College of Animal Science, Jilin University, Changchun, China.
Zhen Weng *College of Animal Science, Jilin University, Changchun, China.
Yuanzhu Zhang *College of Animal Science, Jilin University, Changchun, China.
Zhi CaoCollege of Animal Science, Jilin University, Changchun, China.
Xingjun KeCollege of Animal Science, Jilin University, Changchun, China.
Ruize SunCollege of Animal Science, Jilin University, Changchun, China.
Yin XieCollege of Animal Science, Jilin University, Changchun, China.
Mengjie LianCollege of Animal Science, Jilin University, Changchun, China.
Lin YangCollege of Animal Science, Jilin University, Changchun, China.
Hongming YuanCollege of Animal Science, Jilin University, Changchun, China.ORCID http://orcid.org/0000-0002-0809-5599
Zicong XieCollege of Animal Science, Jilin University, Changchun, China.
HongSheng OuyangCollege of Animal Science, Jilin University, Changchun, China.
Daxin PangCollege of Animal Science, Jilin University, Changchun, China. pdx@jlu.edu.cn.ORCID http://orcid.org/0000-0001-5070-125X
Dongmei LvCollege of Animal Science, Jilin University, Changchun, China. lvdongmei@jlu.edu.cn.ORCID http://orcid.org/0000-0002-9890-4555

Funding

Department of Science and Technology of Jilin Province (Jilin Province Science and Technology Department) 20240303068NCNational Natural Science Foundation of China (National Science Foundation of China) 32372962
6 · The paper itself

Abstract

The continued spread and regular outbreaks of African swine fever (ASF) have severely threatened the pig-related industries, causing economic losses. African swine fever virus (ASFV) encoded more than 150 different proteins, but the biological characteristics of the majority of these proteins remain unknown. In this study, we leveraged the Phage ImmunoPrecipitation Sequencing (PhIp-Seq) platform to perform an exhaustive serological analysis of ASFV to characterize the specific reactivities of serum anti-ASFV IgG antibodies against the ASFV proteome at peptide resolution. High-resolution epitope mapping of the ASFV antigens was conducted, and a total of 29 ASFV antigens with high immunogenicity were identified, 14 of which, to the best of our knowledge, have not been previously identified as serological antigens. The immunogenicity of these 29 antigens was evaluated, and their conservation was statistically analyzed across 169 ASFV strains. We found that the uncharacterized protein DP238L is a conserved antigen that is widely hit within the population. The immunogenicity of DP238L and multi-epitope recombinant proteins was validated by immunoblotting and animal immunization trials, confirming the immunogenicity of the identified antigens and the reliability of the PhIp-Seq based epitope mapping strategy. These findings provide insights into the structures and functions of antigen proteins and identify crucial targets for ASFV detection and vaccine development.

Indexed as

African Swine FeverAfrican Swine Fever VirusAntibodies, ViralAntigens, ViralEpitope MappingPeptide LibraryProteomeAnimalsSwineAntibodies, ViralAntigens, ViralPeptide LibraryProteome

Identifiers

PMID41703287
PMCPMC13022430

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.