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  1. Article: Characterization of T cell hybridomas raised against a glycopeptide containing the tumor-associated T antigen, (betaGal (1-3) alphaGalNAc-O/Ser).

    Gad, Monika / Werdelin, Ole / Meldal, Morten / Komba, Shiro / Jensen, Teis

    Glycoconjugate journal

    2003  Volume 19, Issue 1, Page(s) 59–65

    Abstract: ... associated disaccharide betaGal (1-3) alphaGalNAc (Core-1) O-linked to serine at position 72 in the mouse ... the monosaccharide alphaGalNAc O-linked to serine. In addition, one hybridoma cross-responded to the glycopeptide T ...

    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.
    MeSH term(s) Amino Acid Sequence ; Animals ; Antigens, Viral, Tumor/chemistry ; Antigens, Viral, Tumor/immunology ; Complementarity Determining Regions/chemistry ; Complementarity Determining Regions/immunology ; Dose-Response Relationship, Immunologic ; Female ; Glycopeptides/chemical synthesis ; Glycopeptides/chemistry ; Glycopeptides/immunology ; Hybridomas/immunology ; Mice ; Molecular Sequence Data ; Receptors, Antigen, T-Cell/genetics
    Chemical Substances Antigens, Viral, Tumor ; Complementarity Determining Regions ; Glycopeptides ; Receptors, Antigen, T-Cell
    Language English
    Publishing date 2003-11-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 283770-5
    ISSN 1573-4986 ; 0282-0080
    ISSN (online) 1573-4986
    ISSN 0282-0080
    DOI 10.1023/a:1022537031617
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Carbohydrate and peptide specificity of MHC class II-restricted T cell hybridomas raised against an O-glycosylated self peptide.

    Jensen, T / Hansen, P / Galli-Stampino, L / Mouritsen, S / Frische, K / Meinjohanns, E / Meldal, M / Werdelin, O

    Journal of immunology (Baltimore, Md. : 1950)

    1997  Volume 158, Issue 8, Page(s) 3769–3778

    Abstract: MHC class II E(k)-restricted, IL-2 secreting T cell hybridomas were raised against the synthetic glycopeptide Hb(67-76)-alpha-GalNAc, (T72(Tn)), in CBA/J mice (H-2(k)). The fine specificity of the hybridomas against the glycan moiety was investigated by ... ...

    Abstract MHC class II E(k)-restricted, IL-2 secreting T cell hybridomas were raised against the synthetic glycopeptide Hb(67-76)-alpha-GalNAc, (T72(Tn)), in CBA/J mice (H-2(k)). The fine specificity of the hybridomas against the glycan moiety was investigated by testing their response against a panel of Hb(67-76)-derived glycopeptides, all with a glycan attached to serine or threonine at the position 72 in the peptide, but with different glycans. The hybridomas showed a high degree of specificity for the alpha-GalNAc moiety with few and faint cross-responses to the glycopeptides having other glycans attached even though some of these were structurally very similar to alpha-GalNAc. The fine specificity of the hybridomas for the peptide moiety was investigated by testing their responses to a panel of Hb(67-76)-alpha-GalNAc glycopeptides with alanine substitutions at all positions except at the two MHC binding anchor positions, I68 and K76, and the T72 to which the alpha-GalNAc was attached. Glycopeptides substituted with alanine at positions where the amino acid side chain pointed toward the TCR did not stimulate the hybridomas, whereas glycopeptides substituted with alanine at positions orientated down into the MHC binding groove stimulated many of the hybridomas. These results indicate that the glycan attached to the peptide as well as solvent-accessible parts of the peptide are recognized with a high degree of specificity by the T cells, whereas the parts of the peptide buried in the MHC binding site are less important or totally ignored by the T cells.
    MeSH term(s) Animals ; Antibodies, Monoclonal/immunology ; Antibody Specificity ; Female ; Glycopeptides/immunology ; Histocompatibility Antigens Class II/immunology ; Hybridomas/immunology ; Mice ; Mice, Inbred CBA ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes/immunology
    Chemical Substances Antibodies, Monoclonal ; Glycopeptides ; Histocompatibility Antigens Class II
    Language English
    Publishing date 1997-04-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3056-9
    ISSN 1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
    ISSN (online) 1550-6606
    ISSN 0022-1767 ; 1048-3233 ; 1047-7381
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  3. Article ; Online: Origin of adaptations to open environments and social behaviour in sabretoothed cats from the northeastern border of the Tibetan Plateau.

    Jiangzuo, Qigao / Werdelin, Lars / Sanisidro, Oscar / Yang, Rong / Fu, Jiao / Li, Shijie / Wang, Shiqi / Deng, Tao

    Proceedings. Biological sciences

    2023  Volume 290, Issue 1997, Page(s) 20230019

    Abstract: The iconic ... ...

    Abstract The iconic sabretooth
    MeSH term(s) Animals ; Tibet ; Carnivora ; Acclimatization ; Adaptation, Physiological ; Social Behavior
    Language English
    Publishing date 2023-04-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209242-6
    ISSN 1471-2954 ; 0080-4649 ; 0962-8452 ; 0950-1193
    ISSN (online) 1471-2954
    ISSN 0080-4649 ; 0962-8452 ; 0950-1193
    DOI 10.1098/rspb.2023.0019
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  4. Book: The origin, nature, and specificity of mononuclear cells in experimental autoimmune inflammations

    Werdelin, Ole

    (Acta pathologica et microbiologica Scandinavica : Supplementum ; 232 : Section A)

    1972  

    Series title Acta pathologica et microbiologica Scandinavica : Supplementum ; 232 : Section A
    Acta pathologica et microbiologica Scandinavica
    Acta pathologica et microbiologica Scandinavica ; Supplementum
    Collection Acta pathologica et microbiologica Scandinavica
    Acta pathologica et microbiologica Scandinavica ; Supplementum
    Language English
    Size 91 S. : Ill.
    Publisher Munksgaard
    Publishing place Copenhagen
    Publishing country Denmark
    Document type Book
    HBZ-ID HT001124634
    ISBN 87-16-01145-7 ; 978-87-16-01145-9
    Database Catalogue ZB MED Medicine, Health

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  5. Article: Autoantigen processing and the mechanisms of tolerance to self.

    Werdelin, O

    Immunology series

    1990  Volume 52, Page(s) 1–9

    Abstract: Large foreign protein antigens are processed in antigen presenting cells before they can be recognized by T lymphocytes. The processing involves the ingestion of the antigen, a controlled proteolytic fragmentation, and the association of immunogenic ... ...

    Abstract Large foreign protein antigens are processed in antigen presenting cells before they can be recognized by T lymphocytes. The processing involves the ingestion of the antigen, a controlled proteolytic fragmentation, and the association of immunogenic fragments with MHC class II molecules. The processing provides for exposure to the T lymphocytes of the immune system of epitopes which are buried in the interior of globular protein. Here we argue that autologous molecules (i.e., autoantigens) are also processed and that this applies to intracellular molecules as well as to plasma membrane proteins and tissues and serum proteins. The implication is that autoimmune T lymphocytes recognize fragments of self molecules in the context of MHC molecules and that autotolerance is toward these same epitopes.
    MeSH term(s) Animals ; Antigen-Presenting Cells/immunology ; Autoantigens/metabolism ; Autoimmunity ; Histocompatibility Antigens Class II/metabolism ; Humans ; Immune Tolerance ; Peptide Fragments/immunology ; Peptide Fragments/metabolism ; T-Lymphocytes/immunology ; Thyroid Gland/immunology
    Chemical Substances Autoantigens ; Histocompatibility Antigens Class II ; Peptide Fragments
    Language English
    Publishing date 1990
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 0092-6019
    ISSN 0092-6019
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  6. Article: T cells recognize antigen alone and not MHC molecules.

    Werdelin, O

    Immunology today

    1987  Volume 8, Issue 7-8, Page(s) 203

    Language English
    Publishing date 1987
    Publishing country England
    Document type Letter
    ZDB-ID 283214-8
    ISSN 1355-8242 ; 0167-5699 ; 0167-4919
    ISSN (online) 1355-8242
    ISSN 0167-5699 ; 0167-4919
    DOI 10.1016/0167-5699(87)90162-9
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  7. Article: T cells recognize antigen alone and not MHC molecules.

    Werdelin, O

    Immunology today

    1987  Volume 8, Issue 3, Page(s) 80–84

    Abstract: ... Ole Werdelin argues that this dogma is false. Taking the case of T-cell responses which are controlled ...

    Abstract It is a central dogma of contemporary immunology that T cells engaged in immune responses to foreign antigens or cells recognize determinants on major histocompatibility complex (MHC) molecules. Here Ole Werdelin argues that this dogma is false. Taking the case of T-cell responses which are controlled by MHC class II molecules, he suggests that la molecules serve to bind antigen fragments and stabilize them in the membrane of presenting cells, shielding them from proteolytic degradation and permitting T cells to bind the epitopes so displayed.
    Language English
    Publishing date 1987
    Publishing country England
    Document type Journal Article
    ZDB-ID 283214-8
    ISSN 1355-8242 ; 0167-5699 ; 0167-4919
    ISSN (online) 1355-8242
    ISSN 0167-5699 ; 0167-4919
    DOI 10.1016/0167-5699(87)90850-4
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  8. Article: Determinant protection. A hypothesis for the activity of immune response genes in the processing and presentation of antigens by macrophages.

    Werdelin, O

    Scandinavian journal of immunology

    1986  Volume 24, Issue 6, Page(s) 625–636

    MeSH term(s) Amino Acid Sequence ; Animals ; Antigen-Presenting Cells/physiology ; Antigens/immunology ; Binding Sites ; Epitopes/immunology ; Genes, MHC Class II ; Humans ; Macrophages/physiology ; Peptide Hydrolases/physiology ; T-Lymphocytes/immunology
    Chemical Substances Antigens ; Epitopes ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 1986-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 120476-2
    ISSN 1365-3083 ; 0300-9475
    ISSN (online) 1365-3083
    ISSN 0300-9475
    DOI 10.1111/j.1365-3083.1986.tb02181.x
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  9. Article: Immune response genes.

    Werdelin, O

    Allergy

    1982  Volume 37, Issue 7, Page(s) 451–461

    MeSH term(s) Animals ; Antibody Formation ; Antigens/administration & dosage ; Dinitrobenzenes/immunology ; Genes, MHC Class II ; Guinea Pigs ; H-2 Antigens/genetics ; HLA Antigens/genetics ; Histocompatibility Antigens Class II/immunology ; Humans ; Hypersensitivity, Delayed/immunology ; Lymphocyte Cooperation ; Macaca mulatta ; Macrophages/immunology ; Major Histocompatibility Complex ; Mice ; Polylysine/genetics ; Polylysine/immunology ; Protein Biosynthesis ; Rats ; T-Lymphocytes/immunology
    Chemical Substances Antigens ; Dinitrobenzenes ; H-2 Antigens ; HLA Antigens ; Histocompatibility Antigens Class II ; Polylysine (25104-18-1)
    Language English
    Publishing date 1982-10
    Publishing country Denmark
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 391933-x
    ISSN 1398-9995 ; 0105-4538
    ISSN (online) 1398-9995
    ISSN 0105-4538
    DOI 10.1111/j.1398-9995.1982.tb02328.x
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  10. Article: Chemically related antigens compete for presentation by accessory cells to T cells.

    Werdelin, O

    Journal of immunology (Baltimore, Md. : 1950)

    1982  Volume 129, Issue 5, Page(s) 1883–1891

    Abstract: Immune responsiveness of guinea pigs to dinitrophenyl-poly-L-lysine (DNP-PLL) and to the lysine-rich random copolymer of L-glutamic acid and L-lysine (GL) are both controlled by the "poly-L-lysine gene." We demonstrate that accessory cells of responder ... ...

    Abstract Immune responsiveness of guinea pigs to dinitrophenyl-poly-L-lysine (DNP-PLL) and to the lysine-rich random copolymer of L-glutamic acid and L-lysine (GL) are both controlled by the "poly-L-lysine gene." We demonstrate that accessory cells of responder strains can be made incapable of presenting DNP-PLL to response T cells in assays for proliferation by in vitro exposure of the cells to GL before and during their exposure to DNP-PLL. The inhibition was not rapidly reversible, because GL preexposed accessory cells that were cultured for 2 hr in GL-free medium were still refractory to pulsing with DNP-PLL. In contrast, DNP-PLL had only a moderate inhibitory effect on accessory cell presentation of GL. Unconjugated poly- and oligo-lysines also inhibited the ability of accessory cells to present DNP-PLL, but inhibitory activity was displayed only by homopolymers containing eight to 12 or more residues in the chain. The homopolymers of D-lysine, L-arginine, and L-glutamic acid, and lysine-free glutamic acid-rich copolymers had little or no inhibitory effect. The results are interpreted to mean that antigens to which responsiveness is regulated by the same Ir gene compete for presentation by accessory cells. This may reflect a competition for the Ir gene product of the antigen-presenting cell.
    MeSH term(s) Animals ; Antigens/immunology ; Ascitic Fluid/cytology ; Ascitic Fluid/immunology ; Binding, Competitive ; Dinitrobenzenes/immunology ; Dinitrobenzenes/metabolism ; Dose-Response Relationship, Immunologic ; Female ; Guinea Pigs ; Lymphocyte Activation ; Lymphocyte Cooperation ; Male ; Molecular Weight ; Peptides/genetics ; Polyglutamic Acid/immunology ; Polylysine/genetics ; Polylysine/immunology ; Polylysine/metabolism ; T-Lymphocytes/immunology ; Time Factors
    Chemical Substances Antigens ; Dinitrobenzenes ; Peptides ; Polylysine (25104-18-1) ; Polyglutamic Acid (25513-46-6) ; poly(glutamic acid-lysine) (27456-64-0)
    Language English
    Publishing date 1982-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3056-9
    ISSN 1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
    ISSN (online) 1550-6606
    ISSN 0022-1767 ; 1048-3233 ; 1047-7381
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