Structural Requirements for Recognition of a Type II Collagen Peptide by Murine T Cell Hybridomas

Lambert, Laurie E.; Berling, Jennifer S.

doi:10.1006/cimm.1994.1015

Cited by 8 publications

(9 citation statements)

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“…1 shows the responses of four distinct T cell hybridomas to peptides in which the residues of CII 256-270 were substituted, one by one, by alanine. All four T cell hybridomas recognized a core consisting of CII 260-267, confirming previous data [19], but displayed different fine specificities within this core. Common to the T cell hybridomas was a total loss of reactivity when isoleucine (I260), lysine (K264) or glutamic acid (E266) were substituted by alanines.…”

Section: Results and Discussion 22 T Cell Hybridomassupporting

confidence: 88%

Antigen processing and presentation of a naturally glycosylated protein elicits major histocompatibility complex class II‐restricted, carbohydrate‐specific T cells

et al. 1996

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Antigen processing and presentation of a naturally glycosylated protein elicits major histocompatibility complex class 11-restricted, carbohydrate-specific T cellsIt is well known that T cells recognize antigen as processed peptides bound to major histocompatibility complex molecules on the surface of antigenpresenting cells. Recently, it has been shown that T cells can specifically recognize synthetic glycopeptides. However, whether glycopeptides are selected for presentation during antigen processing of glycoproteins and eventually elicit carbohydrate-specific T cells is still an open question. In this study, we utilized synthetic glycopeptides to analyze T cell recognition of the naturally glycosylated immunodominant peptide representing type I1 collagen (CII) residues 256-270. In this peptide, lysines at positions 264 and 270 may be posttranslationally modified by hydroxylation and subsequent 0-linked glycosylation with P-galactosyl or a-glucosyl-( 1 + 2)-P-galactosyl residues. T cell hybridomas established from type I1 collagen-immunized mice specifically recognized CII 256-270 with either galactose or glucosyl-galactose at position 264. The T cell hybridoma recognizing glucosyl-galactose displayed no cross-reactivity either to galactose or to the structurally different a-galactosyL(1 + 4)4-galactose. Furthermore, the T cell hybridoma recognizing galactose did not cross-react to glucosyl-galactose or galactosyl-galactose, indicating that the antigen-presenting cells (bulk spleen

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Section: Results and Discussion 22 T Cell Hybridomassupporting

confidence: 88%

Antigen processing and presentation of a naturally glycosylated protein elicits major histocompatibility complex class II‐restricted, carbohydrate‐specific T cells

et al. 1996

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“…Alternatively, lengthening of the peptide at the N-terminus may result in an increase of affinity of the peptide to T cell receptor/MHC. It has been demonstrated that CII 255-270 peptide is >100-fold more active than CII 260-270 in stimulating CII 260-270 T cell hybridomas [27]. The use of truncated peptides will also allow us the precise definition of why peptide 259-273 does not apparently induce nasal tolerance.…”

Section: Nasal Tolerance To Collagen-induced Arthritismentioning

confidence: 99%

Differential Activities of Immunogenic Collagen Type II Peptides in the Induction of Nasal Tolerance to Collagen-Induced Arthritis

Chu

Londei

1999

Journal of Autoimmunity

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“…The central core has been suggested to be located between position 260 and 270, in which substitution of positions 260-264 and 266 abolished or reduced T cell stimulation [10,[12][13][14]. Furthermore, N-terminal prolongation of the CII 260-270 peptide, including position 256, enhanced the stimulation of many T cells [8,15]. There are two prerequisites for the immunodominance of the CII 256-270 peptide.…”

Section: Introductionmentioning

confidence: 99%

The structural basis of MHC control of collagen-induced arthritis; binding of the immunodominant type II collagen 256 – 270 glycopeptide to H-2Aq and H-2Ap molecules

et al. 1998

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The Aq major histocompatibility complex (MHC) class II molecule is associated with susceptibility to murine collagen-induced arthritis (CIA), whereas the closely related H-2Ap molecule is not. To understand the molecular basis for this difference, we have analyzed the ability of H-2Aq and H-2Ap molecules (referred to as Aq and Ap) to bind and present collagen type II (CII)-derived glycosylated and non-glycosylated peptides. T cell clones specific for the immunodominant CII 256-270 peptide and restricted to both Aq and Ap molecules were identified. When these clones were incubated with CII protein and either Aq- or Ap-expressing antigen-presenting cells (APC), only Aq-expressing APC were able to induce stimulation. With the use of A(beta) transgenic mice this could be shown to be solely dependent on the MHC class II molecule itself and to be independent of other MHC- or non-MHC genes. Peptide binding studies were performed using affinity-purified MHC class II molecules. The CII 256-270 peptide bound with lower affinity to the Ap molecule than to the Aq molecule. Using a set of alanine-substituted CII 256-270 peptides, MHC class II and T cell receptor (TCR) contacts were identified. Mainly the side chains of isoleucine 260 and phenylalanine 263 were used for binding both the Aq and Ap molecule, i.e. the peptide was orientated similarly in the binding clefts. The major TCR contact amino acids were lysine 264, which can be posttranslationally modified, and glutamic acid 266, which is the only amino acid in the heterologous peptide which differs from the mouse sequence. Glycosylation at positions 264 and 270 of the CII 256-270 peptide did not change the anchor positions used for binding to the Aq or Ap molecules. The autologous form of the peptide (with aspartic acid at position 266) bound with lower affinity to the Aq molecule as compared with the heterologous peptide. The variable affinity displayed by the immunodominant CII 256-270 peptide for different MHC class II molecules, the identification of MHC and TCR contacts and the significance of glycosylation of these have important implications for the understanding of the molecular basis for inherited MHC class II-associated susceptibility to CIA and in turn, for development of novel treatment strategies in this disease.

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Structural Requirements for Recognition of a Type II Collagen Peptide by Murine T Cell Hybridomas

Cited by 8 publications

References 0 publications

Antigen processing and presentation of a naturally glycosylated protein elicits major histocompatibility complex class II‐restricted, carbohydrate‐specific T cells

Antigen processing and presentation of a naturally glycosylated protein elicits major histocompatibility complex class II‐restricted, carbohydrate‐specific T cells

Differential Activities of Immunogenic Collagen Type II Peptides in the Induction of Nasal Tolerance to Collagen-Induced Arthritis

The structural basis of MHC control of collagen-induced arthritis; binding of the immunodominant type II collagen 256 – 270 glycopeptide to H-2Aq and H-2Ap molecules

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