Evidence map›Paper›PMID 41238631›Full record

ArticleCommunications biology2025

Structures of CRP antigen-antibody complexes provide insights into the mechanism of specific recognition.

Yijian Li, Qianxi Yu, Mengtan Du, Jian Zhang, Tonggong Liu, Jingzhe Wang, Qingchun Wei, Yong Peng, Chaohui Duan, Dayong Gu and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Yijian LiDepartment of Laboratory Medicine, Shenzhen Key Laboratory of Medical Laboratory and Molecular Diagnostics, Shenzhen Institute of Translational Medicine, The First Affiliated Hospital of Shenzhen University, Shenzhen Second People's Hospital, Shenzhen, China.ORCID http://orcid.org/0000-0003-1416-4535
Qianxi YuDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, China.
Mengtan DuDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, China.
Jian ZhangDepartment of Laboratory Medicine, Shenzhen Key Laboratory of Medical Laboratory and Molecular Diagnostics, Shenzhen Institute of Translational Medicine, The First Affiliated Hospital of Shenzhen University, Shenzhen Second People's Hospital, Shenzhen, China.
Tonggong LiuDepartment of Laboratory Medicine, Shenzhen Key Laboratory of Medical Laboratory and Molecular Diagnostics, Shenzhen Institute of Translational Medicine, The First Affiliated Hospital of Shenzhen University, Shenzhen Second People's Hospital, Shenzhen, China.
Jingzhe WangDepartment of Laboratory Medicine, Shenzhen Key Laboratory of Medical Laboratory and Molecular Diagnostics, Shenzhen Institute of Translational Medicine, The First Affiliated Hospital of Shenzhen University, Shenzhen Second People's Hospital, Shenzhen, China.
Qingchun WeiDepartment of Laboratory Medicine, Shenzhen Yantian District People's Hospital, Shenzhen, China.
Yong PengBeijing Sjodax Biotechnology, Beijing, China.
Chaohui DuanDepartment of Clinical Laboratory, Sun Yat-sen Memorial Hospital, Sun Yat-sen University, Guangzhou, Guangdong, China. duanchh@mail.sysu.edu.cn.ORCID http://orcid.org/0000-0003-3130-5045
Dayong GuDepartment of Laboratory Medicine, Shenzhen Key Laboratory of Medical Laboratory and Molecular Diagnostics, Shenzhen Institute of Translational Medicine, The First Affiliated Hospital of Shenzhen University, Shenzhen Second People's Hospital, Shenzhen, China. wanhood@163.com.ORCID http://orcid.org/0000-0002-9547-8474
Fuxing ZengDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, China. zengfx@sustech.edu.cn.ORCID http://orcid.org/0000-0003-0790-0151

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antigen-antibody specific recognition constitutes fundamental research in molecular drug design and immune diagnostics, where cumulative non-covalent interactions critically determine binding affinities. Current mechanistic understanding of antibody affinity optimization remains incomplete, hindering rational structure-based design of therapeutic antibodies and bispecific variants. This study presents four cryo-EM structures of C-reactive protein (CRP) complexed with heavy-chain antibodies (HCAbs) of varying affinities, resolved at 3.0-3.4 Å resolution. Comparative structural analysis reveals pronounced variations in binding modalities among affinity-differentiated HCAbs, while identifying critical determinants of engagement conformations, providing mechanistic insights for rational optimization of CRP-specific antibodies.

Indexed as

Antigen-Antibody ComplexC-Reactive ProteinAntibody AffinityCryoelectron MicroscopyHumansImmunoglobulin Heavy ChainsModels, MolecularProtein BindingProtein ConformationAntigen-Antibody ComplexC-Reactive ProteinImmunoglobulin Heavy Chains

Identifiers

PMID41238631
PMCPMC12618693

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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.