ArticleProceedings of the National Academy of Sciences of the United States of America2010
Antibody recognition of a unique tumor-specific glycopeptide antigen.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
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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.
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Who cites it
46 citing papers in PubMed, 86 citations in OpenAlex.
- Structural Basis of a High-Affinity Antibody Binding to Glycoprotein with Glycocalyx Decay.JACS Au · 2026Article
- From Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer.Chemical reviews · 2026Review
- Cancer-associated alterations in O-GalNAc glycosylation.Glycobiology · 2026Review
- Dual-recognizing antibodies targeting CEACAMs in the tumor microenvironment: towards more precise targeting.Cell communication and signaling : CCS · 2026Review
- Integrative Approach to Develop and Characterize Antibodies against the Cancer-Associated Antigen Sialyl Lewis A (CA 19-9).JACS Au · 2026Article
- Structural Basis for Multivalent MUC16 Recognition and Robust Anti-Pancreatic Cancer Activity of Humanized Antibody AR9.6.Molecular cancer therapeutics · 2024Article
- Identification of the glycopeptide epitope recognized by a protectiveInfection and immunity · 2023Article
- Targeting Solid Cancers with a Cancer-Specific Monoclonal Antibody to Surface Expressed Aberrantly O-glycosylated Proteins.Molecular cancer therapeutics · 2023Article
- Review
- Review
- Mechanism of glycoform specificity and in vivo protection by an anti-afucosylated IgG nanobody.Nature communications · 2023Article
- Single CAR-T cell treatment controls disseminated ovarian cancer in a syngeneic mouse model.Journal for immunotherapy of cancer · 2023Article
- Molecular Recognition of GalNAc in Mucin-Type O-Glycosylation.Accounts of chemical research · 2023Review
- Synthesis and biomedical applications of mucin mimic materials.Advanced drug delivery reviews · 2022Review
- Synthetic nanobodies as tools to distinguish IgG Fc glycoforms.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Review
- Potential of Anti-MUC1 Antibodies as a Targeted Therapy for Gastrointestinal Cancers.Vaccines · 2020Review
- Structure-guided engineering of the affinity and specificity of CARs against Tn-glycopeptides.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Aberrantly glycosylated integrin α3β1 is a unique urinary biomarker for the diagnosis of bladder cancer.Aging · 2020Article
- A straightforward approach to antibodies recognising cancer specific glycopeptidic neoepitopes.Chemical science · 2020Article
Corrections and comments
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Authors and funding
10 authors at 8 institutions in 3 countries.
Funding
Abstract
Aberrant glycosylation and the overexpression of certain carbohydrate moieties is a consistent feature of cancers, and tumor-associated oligosaccharides are actively investigated as targets for immunotherapy. One of the most common aberrations in glycosylation patterns is the presentation of a single O-linked N-acetylgalactosamine on a threonine or serine residue known as the "Tn antigen." Whereas the ubiquitous nature of Tn antigens on cancers has made them a natural focus of vaccine research, such carbohydrate moieties are not always tumor-specific and have been observed on embryonic and nonmalignant adult tissue. Here we report the structural basis of binding of a complex of a monoclonal antibody (237mAb) with a truly tumor-specific glycopeptide containing the Tn antigen. In contrast to glycopeptide-specific antibodies in complex with simple peptides, 237mAb does not recognize a conformational epitope induced in the peptide by sugar substitution. Instead, 237mAb uses a pocket coded by germ-line genes to completely envelope the carbohydrate moiety itself while interacting with the peptide moiety in a shallow groove. Thus, 237mAb achieves its striking tumor specificity, with no observed physiological cross-reactivity to the unglycosylated peptide or the free glycan, by a combination of multiple weak but specific interactions to both the peptide and to the glycan portions of the antigen.
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Registered trials
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.