Evidence map›Paper›PMID 23604173›Full record

ArticleCancer immunology, immunotherapy : CII2013

Monoclonal antibodies toward different Tn-amino acid backbones display distinct recognition patterns on human cancer cells. Implications for effective immuno-targeting of cancer.

Daniel Mazal, Richard Lo-Man, Sylvie Bay, Otto Pritsch, Edith Dériaud, Christelle Ganneau, Andrea Medeiros, Luis Ubillos, Gonzalo Obal, Nora Berois and 3 more

Open access · greenAbstract read
In one paragraph

Article in Cancer immunology, immunotherapy : CII, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.2field-weighted citation impact, top 12% of its field
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

26 citing papers in PubMed, 44 citations in OpenAlex.

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  18. Heterovalent Glycodendrimers as Epitope Carriers for Antitumor Synthetic Vaccines.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017
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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

13 authors at 5 institutions in 4 countries.

Daniel MazalDepartamento de Anatomía Patológica y Citología del Hospital de la Mujer, Centro Hospitalario Pereira Rossell, Montevideo, Uruguay.
Richard Lo-Man
Sylvie Bay
Otto Pritsch
Edith Dériaud
Christelle Ganneau
Andrea Medeiros
Luis Ubillos
Gonzalo Obal
Nora Berois
Mariela Bollati-Fogolin
Claude Leclerc
Eduardo Osinaga
Universidad de la República de Uruguay · UYInserm · FRCentre National de la Recherche Scientifique · FRInstitut Pasteur · FRCentro Hospitalario Pereira Rossell · UY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Tn antigen (GalNAcα-O-Ser/Thr) is a well-established tumor-associated marker which represents a good target for the design of anti-tumor vaccines. Several studies have established that the binding of some anti-Tn antibodies could be affected by the density of Tn determinant or/and by the amino acid residues neighboring O-glycosylation sites. In the present study, using synthetic Tn-based vaccines, we have generated a panel of anti-Tn monoclonal antibodies. Analysis of their binding to various synthetic glycopeptides, modifying the amino acid carrier of the GalNAc(*) (Ser* vs Thr*), showed subtle differences in their fine specificities. We found that the recognition of these glycopeptides by some of these MAbs was strongly affected by the Tn backbone, such as a S*S*S* specific MAb (15G9) which failed to recognize a S*T*T* or a T*T*T* structure. Different binding patterns of these antibodies were also observed in FACS and Western blot analysis using three human cancer cell lines (MCF-7, LS174T and Jurkat). Importantly, an immunohistochemical analysis of human tumors (72 breast cancer and 44 colon cancer) showed the existence of different recognition profiles among the five antibodies evaluated, demonstrating that the aglyconic part of the Tn structure (Ser vs Thr) plays a key role in the anti-Tn specificity for breast and colon cancer detection. This new structural feature of the Tn antigen could be of important clinical value, notably due to the increasing interest of this antigen in anticancer vaccine design as well as for the development of anti-Tn antibodies for in vivo diagnostic and therapeutic strategies.

Indexed as

AdultAgedAged, 80 and overAmino Acid SequenceAnimalsAntibodies, MonoclonalAntibody SpecificityAntigens, Tumor-Associated, CarbohydrateBiomarkers, TumorBreast NeoplasmsCell Line, TumorColonic NeoplasmsFemaleGlycopeptidesHumansMaleAntibodies, MonoclonalAntigens, Tumor-Associated, CarbohydrateBiomarkers, TumorGlycopeptidesTn antigen

Identifiers

PMID23604173
PMCPMC11029704
OpenAlexW2032283616

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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.