Evidence map›Paper›PMID 40845830›Full record

ArticleCell chemical biology2025

Engineering affinity-matured variants of an anti-polysialic acid monoclonal antibody with superior cytotoxicity-mediating potency.

Weiyao Wang, Mehman Bunyatov, Deana Moffat, Natalia Lopez-Barbosa, Matthew P DeLisa

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell chemical biology, 2025. 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. Review
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Weiyao WangRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, Olin Hall, Ithaca, NY 14853, USA.
Mehman BunyatovRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, Olin Hall, Ithaca, NY 14853, USA.
Deana MoffatNancy E. and Peter C. Meinig School of Biomedical Engineering School of Biomedical Engineering, Cornell University, Olin Hall, Ithaca, NY 14853, USA.
Natalia Lopez-BarbosaRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, Olin Hall, Ithaca, NY 14853, USA.
Matthew P DeLisaRobert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, Olin Hall, Ithaca, NY 14853, USA; Nancy E. and Peter C. Meinig School of Biomedical Engineering School of Biomedical Engineering, Cornell University, Olin Hall, Ithaca, NY 14853, USA; Cornell Institute of Biotechnology, Cornell University, 130 Biotechnology Building, Ithaca, NY 14853, USA. Electronic address: md255@cornell.edu.

Funding

Molecular toolkit for high content resolution of glycomes by expansionmicroscopyR01GM137314 · NIGMS · CORNELL UNIVERSITY · PI ALABI, CHRISTOPHER AKINLEYE, DELISA, MATTHEW P · 2020 to 2023
$1.8M
High-throughput label-free detection system for biomolecular interaction analysisS10OD032273 · OD · CORNELL UNIVERSITY · PI DELISA, MATTHEW P · 2022 to 2022
$350k
NIGMS NIH HHS R01 GM137314NIH HHS S10 OD032273
6 · The paper itself

Abstract

Monoclonal antibodies (mAbs) that specifically recognize cell surface glycans associated with cancer and infectious disease hold tremendous value for basic research and clinical applications. However, high-quality anti-glycan mAbs with sufficiently high affinity and specificity remain scarce, highlighting the need for strategies that enable optimization of antigen-binding properties. To this end, we engineered the affinity of a polysialic acid (polySia)-specific antibody called mAb735, which possesses only modest affinity. Using a combination of rational design and directed evolution, we isolated several affinity-matured IgG variants with ∼5- to 7-fold stronger affinity for polySia relative to mAb735. The higher affinity IgG variants opsonized polySia-positive cancer cells more avidly and triggered greater antibody-dependent cell-mediated cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC). Collectively, these results demonstrate the effective application of molecular evolution techniques to an important anti-glycan antibody, providing insights into its carbohydrate recognition and uncovering variants with greater therapeutic promise due to their enhanced affinity and potency.

Indexed as

Antibodies, MonoclonalProtein EngineeringSialic AcidsAnimalsAntibody AffinityAntibody-Dependent Cell CytotoxicityCell Line, TumorHumansAntibodies, Monoclonalpolysialic acidSialic Acidsaffinity maturationcancercapsular polysaccharidesdirected evolutionglycoproteinglycosylationmonoclonal antibodiesTACAtumor-associated carbohydrate antigenyeast surface display

Identifiers

PMID40845830
PMCPMC12812327

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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.