Heterogeneity of HLA-B7 as Detected by Cytotoxic T Cell Clones

Seventer, G van; Ijssel, H; Breuning, Martijn H.; Spits, Hergen; Breur, B. S.; Poelgeest, A. Van; Huis, B.; Voordouw, A. C.; Iványi, P

doi:10.1007/978-3-642-69770-8_168

Cited by 4 publications

(3 citation statements)

References 2 publications

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“…Nevertheless, p56ICk can associate with the NKR-P1 receptor of rodent NK cells and may play a role in stimulatory signaling through that receptor. It is interesting to note that the pS6Ick interactions with both CD8a and NKR-P1 are of lower apparent affinity and that both receptors are involved in cytolytic effector functions [5,31,321. It is possible that this weaker association provides these receptors (or co-receptors) with a higher trigger threshold for cytolytic activation as opposed to the apparent higher affinity interaction with CD4 that functions as a coreceptor for helper functions.…”

Section: Discussionmentioning

confidence: 99%

The cytoplasmic domain of rat NKR‐P1 receptor interacts with the N‐terminal domain of p56^lck via cysteine residues

Campbell¹,

Giorda²

1997

Eur J Immunol

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NKR-P1 is a type II transmembrane protein which acts as an activation receptor on natural killer (NK) cells. The cytoplasmic domains of the CD4, CD8 and 4-1BB receptors contain the sequence Cys-X-Cys-Pro which is directly involved in coupling to another pair of cysteines in the N-terminal domain of the src family tyrosine kinase p56(lck). The cytoplasmic domain of NKR-P1 in rodents also contains the Cys-X-Cys-Pro sequence, but the capacity of the receptor to bind p56(lck) is presently unknown. We tested for direct coupling between these proteins using both protein biochemistry and the yeast two-hybrid technique. Immunoprecipitation studies showed that p56(lck) can be co-immunoprecipitated with NKR-P1 from a rat NK tumor cell line. In addition, the cytoplasmic domain of NKR-P1 interacted with the N-terminal domain of p56(lck) in yeast as assessed by reporter gene activation. Integrity of the cysteine pairs in both proteins was critical in mediating the interaction. The experiments suggest that the association of p56(lck) with NKR-P1 is somewhat weaker than the p56(lck) association with CD8alpha, but of much lower avidity than between CD4 and p56(lck). This could reflect a higher activation threshold for the NKR-P1 and CD8 receptors, which are involved in cytolytic responses, compared to CD4 which is involved in T cell helper function.

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Section: Discussionmentioning

confidence: 99%

The cytoplasmic domain of rat NKR‐P1 receptor interacts with the N‐terminal domain of p56^lck via cysteine residues

Campbell¹,

Giorda²

1997

Eur J Immunol

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“…Our data show that CD2 mAb-induced nonspecific cytotoxicity of CTL can also be inhibited by CD3 mAb. The reported absence of CD8 involvement in the CD2 mAb-induced nonspecific cytotoxicity as reported by Siliciano et al [20] can be explained either by too strong a triggering signal provided by their experimental combination of CD2 mAb or by functional differences between the epitopes recognized by the various CD8 mAb [7,161 (Fig. 5).…”

Section: -mentioning

confidence: 79%

Regulatory role of the CD8 antigen in both CD3 and CD2 monoclonal antibody‐induced nonspecific cytotoxicity of class I‐ and class II‐allospecific cytotoxic T cell clones

Seventer

Lier²,

Kuijpers

et al. 1988

Eur J Immunol

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We investigated the function of the CD8 moiety in antigen-specific and alternative activation of HLA class I- and HLA class II-allospecific CD8+ cytotoxic T lymphocyte (CTL) clones. Monoclonal antibodies (mAb) directed against the CD8 structure were only found to inhibit antigen-specific cytotoxicity of class I-allospecific CD8+ CTL clones and not of a class II-allospecific CD8+ CTL clone. However, cytotoxicity induced by CD3 mAb (used at suboptimal concentrations) or CD2 mAb in both types of CTL clone was blocked by CD8 mAb. The class II-allospecific CD8+ CTL clone was uniformly more difficult to inhibit than the class I-allospecific CD8+ CTL clones and, moreover, also easier to induce to exert nonspecific cytotoxicity by CD2 mAb and CD3 mAb. The absence of CD8 mAb blocking of antigen-specific cytotoxicity of the class II-specific CD8+ CTL clone is, therefore, assumed to result from too strong a triggering signal to be overcome by the down-regulatory signal of the CD8 antigen. These combined findings suggest a down-regulatory function of CD8 not only in T cell receptor (TcR)/CD3 activation, but also in TcR/CD3-controlled alternative activation routes such as the CD2 activation pathway.

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“…However, little is known about the relevance of particular regions of the molecule in determining the specificity of CTL recognition and MHC restriction. A way of approaching this issue takes advantage of the fact that various well-defined serological specificities may be further divided into several subtypes by specific CTL (7)(8)(9)(10)(11)(12)(13)(14). Detailed biochemical analyses of some of these naturally occurring variants (15)(16)(17)(18)(19) have shown that the different subsets of a given serological specificity differ from each other in a very limited number of amino acid residues.…”

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confidence: 99%

Structural analysis of an HLA-B27 functional variant: identification of residues that contribute to the specificity of recognition by cytolytic T lymphocytes.

Vega¹,

Ezquerra²,

Rojo³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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Heterogeneity of HLA-B7 as Detected by Cytotoxic T Cell Clones

Cited by 4 publications

References 2 publications

The cytoplasmic domain of rat NKR‐P1 receptor interacts with the N‐terminal domain of p56^lck via cysteine residues

The cytoplasmic domain of rat NKR‐P1 receptor interacts with the N‐terminal domain of p56^lck via cysteine residues

Regulatory role of the CD8 antigen in both CD3 and CD2 monoclonal antibody‐induced nonspecific cytotoxicity of class I‐ and class II‐allospecific cytotoxic T cell clones

Structural analysis of an HLA-B27 functional variant: identification of residues that contribute to the specificity of recognition by cytolytic T lymphocytes.

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Heterogeneity of HLA-B7 as Detected by Cytotoxic T Cell Clones

Cited by 4 publications

References 2 publications

The cytoplasmic domain of rat NKR‐P1 receptor interacts with the N‐terminal domain of p56lck via cysteine residues

The cytoplasmic domain of rat NKR‐P1 receptor interacts with the N‐terminal domain of p56lck via cysteine residues

Regulatory role of the CD8 antigen in both CD3 and CD2 monoclonal antibody‐induced nonspecific cytotoxicity of class I‐ and class II‐allospecific cytotoxic T cell clones

Structural analysis of an HLA-B27 functional variant: identification of residues that contribute to the specificity of recognition by cytolytic T lymphocytes.

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The cytoplasmic domain of rat NKR‐P1 receptor interacts with the N‐terminal domain of p56^lck via cysteine residues

The cytoplasmic domain of rat NKR‐P1 receptor interacts with the N‐terminal domain of p56^lck via cysteine residues