Evidence map›Paper›PMID 42824843›Full record

ArticleJournal of oral microbiology2026

Anti-FimA monoclonal antibodies reveal dual roles in porphyromonas gingivalis pathogenesis.

Mingya Cao, Yichang Gao, Siyu Wang, Chengye He, Jieyu Zhang, Min Yan, Shengke Zhou, Zihan Zhao, Yuanyuan Pan, Han Wang and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of oral microbiology, 2026. 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

12 authors.

Mingya CaoJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Yichang GaoJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Siyu WangJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Chengye HeJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Jieyu ZhangJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Min YanJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Shengke ZhouJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Zihan ZhaoJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Yuanyuan PanJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Han WangJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Jingying ChenJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.
Xia LiJoint National Laboratory for Antibody Drug Engineering, College of Synthetic Biology and Pharmaceutical Engineering, Henan University, Kaifeng, People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Objective: To generate and functionally characterize FimA-targeting monoclonal antibodies (mAbs) and define their functional impact on Design: Mice were immunized with recombinant FimA (rFimA) protein to generate hybridomas producing high-affinity mAbs that recognize distinct, non-overlapping epitopes. The functional effects of these mAbs on Results: A panel of high-affinity anti-FimA mAbs targeting distinct, non-overlapping epitopes was generated. Although all mAbs blocked bacterial adhesion and enhanced phagocytosis, they showed limited complement-dependent killing and, paradoxically, induced aggregation that promoted structured biofilm formation. Conclusion: Anti-FimA mAbs exert a dual and opposing functionality, conferring host protection while paradoxically enhancing bacterial persistence through biofilm promotion. These findings reveal a previously unrecognized complexity in anti-FimA humoral immunity and provide important insights for the design of targeted immunotherapies against

Indexed as

FimAfimbriaemonoclonal antibodiesperiodontitisP. gingivalis

Identifiers

PMID42824843
PMCPMC13629768

What OpenQuestion holds

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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.