Evidence map›Paper›PMID 41150750›Full record

ArticleCurrent issues in molecular biology2025

Phage Display Reveals VLRB-Mediated Recognition of Minimal Tumor Glycan Antigen Sialyl-Tn.

Mark Rickard N Angelia, Abigail Joy D Rodelas-Angelia, Youngrim Kim, Cheolung Yang, Hyeok Jang, Seungpyo Jeong, Jihyun Mun, Kim D Thompson, Taesung Jung

Abstract read
In one paragraph

Article in Current issues in molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

9 authors.

Mark Rickard N AngeliaLaboratory of Aquatic Animal Diseases, Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, 501, Jinju-Daero, Jinju-si 52828, Republic of Korea.
Abigail Joy D Rodelas-AngeliaLaboratory of Aquatic Animal Diseases, Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, 501, Jinju-Daero, Jinju-si 52828, Republic of Korea.
Youngrim KimLaboratory of Aquatic Animal Diseases, Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, 501, Jinju-Daero, Jinju-si 52828, Republic of Korea.
Cheolung YangLaboratory of Aquatic Animal Diseases, Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, 501, Jinju-Daero, Jinju-si 52828, Republic of Korea.ORCID 0009-0008-1148-0261
Hyeok JangLaboratory of Aquatic Animal Diseases, Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, 501, Jinju-Daero, Jinju-si 52828, Republic of Korea.
Seungpyo JeongLaboratory of Aquatic Animal Diseases, Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, 501, Jinju-Daero, Jinju-si 52828, Republic of Korea.
Jihyun MunLaboratory of Aquatic Animal Diseases, Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, 501, Jinju-Daero, Jinju-si 52828, Republic of Korea.
Kim D ThompsonMoredun Research Institute, Pentlands Science Park, Bush Loan, Midlothian EH26 0PZ, UK.ORCID 0000-0003-3550-4842
Taesung JungLaboratory of Aquatic Animal Diseases, Institute of Animal Medicine, College of Veterinary Medicine, Gyeongsang National University, 501, Jinju-Daero, Jinju-si 52828, Republic of Korea.ORCID 0000-0001-6028-0946

Funding

The National Research Foundation of Korea RS-2023-00235511, R1A2B5B02002220
6 · The paper itself

Abstract

Sialyl-Tn (sTn) is a tumor-associated carbohydrate antigen (TACA) abundantly expressed by various types of carcinomas. While conventional antibody-based platforms have traditionally been used for the detection and targeting of sTn, alternative binding scaffolds may offer distinct advantages. Variable lymphocyte receptor B (VLRB), the immunoglobulin-like molecule of jawless vertebrates, offers a promising alternative for glycan recognition. In this study, a phage-displayed VLRB library was utilized to identify sTn-specific binders. Two candidates, designated as ccombodies A8 and B11, were isolated after four rounds of biopanning. Both were expressed and purified using Ni-affinity and FPLC, yielding proteins with apparent molecular weights of ~27 kDa in SDS-PAGE. Sequence analysis revealed a preference for glycan-binding residues in randomized hypervariable regions, with A8 exhibiting an increased aliphatic content. ELISA confirmed selective binding to sTn and other

Indexed as

glycan-bindingphage displaysialyl TnTACAvariable lymphocyte receptor

Identifiers

PMID41150750
PMCPMC12562327

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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.