Evidence map›Paper›PMID 41761907›Full record

ArticleNucleic acids research2026

Structural basis of B-to-Z DNA transition mediated by an anti-Z-DNA antibody.

Cheng-Chung Lee, Shu-Fang Hsu, Ya-Wen Chang, Ya-Wen Chen, Meng-Ru Ho, Hiroshi Sugiyama, Wei-Chu Wang, Andrew H-J Wang

Abstract read
In one paragraph

Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Imaging nucleic acids in biofilms.Essays in biochemistry · 2026
    Review
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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

8 authors.

Cheng-Chung LeeThe Ph.D. Program for Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei 110301, Taiwan.ORCID 0000-0002-8259-4388
Shu-Fang HsuThe Ph.D. Program for Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei 110301, Taiwan.ORCID 0000-0002-4818-7260
Ya-Wen ChangThe Ph.D. Program for Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei 110301, Taiwan.
Ya-Wen ChenThe Ph.D. Program for Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei 110301, Taiwan.
Meng-Ru HoInstitute of Biological Chemistry, Academia Sinica, Taipei 115201, Taiwan.
Hiroshi SugiyamaDepartment of Chemistry, Graduate School of Science, Kyoto University, Kitashirakawa-Oiwakecho, Sakyo-Ku, Kyoto 606-8502, Japan.ORCID 0000-0001-8923-5946
Wei-Chu WangThe Ph.D. Program for Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei 110301, Taiwan.ORCID 0000-0002-5452-5537
Andrew H-J WangThe Ph.D. Program for Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei 110301, Taiwan.ORCID 0000-0002-0016-5337

Funding

National Science and Technology CouncilNational Science and Technology Council 112-2311-B-038-002National Science and Technology Council 113-2320-B-038-022-MY3National Science and Technology Council 114-2314-B-038-010National Science and Technology Council 114-2314-B-038-011National Science and Technology Council 114-2320-B-038-009NSTC 114-2811-B-038-022NSTC 114-2811-B-038-026Taipei Medical University
6 · The paper itself

Abstract

Z-DNA is a left-handed double-helical form of DNA that plays roles in transcription, immune responses, viral infection, bacterial biofilm formation, and autoimmune diseases. Despite its importance, the instability of Z-DNA under physiological conditions has hindered detailed structural and functional investigations. Moreover, although antibodies are known to recognize nucleic acids, the mechanisms underlying their detection and stabilization of dynamic DNA under biological conditions remain unclear. This study provides the first atomic-level structural insights into antibody-mediated B-to-Z DNA transition. Accordingly, a Z-DNA-specific chimeric Fab fragment of Z22 (cZ22-Fab) was designed and characterized using multiple biophysical approaches. cZ22-Fab mediates a concentration-dependent B-to-Z conformational transition in CG-repeat DNA, establishing a stable 2:1 Fab/DNA stoichiometry. Crystal structure of cZ22-Fab/Z-DNA complexes revealed a left-handed DNA backbone-tracking recognition mode, in which cZ22-Fab recognizes Z-DNA conformation through phosphate-clamping and base interactions. Notably, a 5'-end C-hanging Z-DNA duplex structure formed by dC(GC)3 and stabilized by cZ22-Fab was observed. Structure-guided mutagenesis demonstrated that heavy chain residues R50 and Y106 are critical for Z-DNA binding, and analyses of additional Z-DNA-forming sequences further elucidated the binding characteristics. Overall, this work provides molecular insights into the mechanism of antibody-mediated Z-DNA formation and stabilization, highlighting its therapeutic relevance and implications for autoimmunity.

Indexed as

DNA, B-FormDNA, Z-FormImmunoglobulin Fab FragmentsCrystallography, X-RayModels, MolecularNucleic Acid ConformationDNA, B-FormDNA, Z-FormImmunoglobulin Fab Fragments

Identifiers

PMID41761907
PMCPMC12956351

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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.