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Cited by 7Glycosylation and Glycoproteins ResearchCarbohydrate Chemistry and SynthesisImmunotherapy and Immune Responses

The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.

Characterization of T cell hybridomas raised against a glycopeptide containing the tumor-associated T antigen, (βGal (1–3) αGalNAc-O/Ser)

Gad, Monika, Werdelin, Ole, Meldal, Morten, Komba, Shiro, Jensen, Teis·2002·Glycoconjugate Journal
DOI 10.1023/a:1022537031617
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Abstract

T cell hybridomas were raised against the glycopeptide S(72) (Core-1) containing the tumor-associated disaccharide betaGal (1-3) alphaGalNAc (Core-1) O-linked to serine at position 72 in the mouse hemoglobin derived decapeptide Hb (67-76). All hybridomas recognized the glycopeptide S(72) (Core-1). Two of the selected hybridomas responded, however, much better to the S(72) (Tn) glycopeptide containing the monosaccharide alphaGalNAc O-linked to serine. In addition, one hybridoma cross-responded to the glycopeptide T(72) (Core-1) having a threonine at position 72 instead of a serine. No cross-responses were found to other glycopeptides consisting of the same hemoglobin peptide with different glycans attached or to the unglycosylated peptides. The T cell receptor Valpha and Vbeta usage was clearly diverse. The CDR3alpha regions demonstrated moreover a predominance of small polar amino acid side chains, and three hybridomas contained a common sequence motif. All the sequenced CDR3beta regions contained furthermore a conserved proline-glycine motif. In conclusion, immunization with the disaccharide containing glycopeptides S(72) (Core-1) created a heterogeneous population of glycopeptide specific T cells with the ability of cross-responding toward related glycopeptides.

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Crossref · 10.1023/a:1022537031617

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Cites

Research works printed but not linked: 1

  1. Galli-Stampino L, Meinjohanns E, Frische K, Meldal M, Jensen T, Werdelin O, Mouritsen S, T-cell recognition of tumor-associated T cell hybridomas recognizing a T-antigen containing glycopeptide 65 carbohydrates: The nature of the glycan moiety plays a decisive role in determining glycopeptide immunogenicity, Cancer Res 57, 3214–22 (1997).

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Metadata

Authors
Gad, M., Werdelin, O., Meldal, M., Komba, S., & Jensen, T.
Affiliations
  • University of Copenhagen (DK)
  • Carlsberg Laboratory (DK)
Corresponding author
Jensen, Teis
ORCID
Venue
Glycoconjugate Journal
Publisher
Springer Science and Business Media LLC
Published
2002-01
Volume
19
Issue
1
Pages
59-65
ISSN
  • 0282-0080 (ISSN-L)
  • 1573-4986
DOI
10.1023/a:1022537031617
OpenAlex
W260342645
Cited by
7
References
35
Citations by year
2023: 1 · 2016: 2 · 2015: 1 · 2013: 2
FWCI
0.00
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Glycoconjugate Journal (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
  • Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
Keywords
T cell hybridomas, Tn antigen, cross-reactivity, T cell receptor CDR3, carbohydrate recognition
MeSH terms
Amino Acid Sequence, Animals, Antigens, Viral, Tumor, Dose-Response Relationship, Immunologic, Female, Glycopeptides, Hybridomas, Molecular Sequence Data, Receptors, Antigen, T-Cell, Complementarity Determining Regions, Mice

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