Immunological function of HLA-C antigens in HLA-Cw3 transgenic mice.

Dill, Othmar; Kievits, F.; Koch, Susanne; Iványi, P; Hämmerling, Günter J.

doi:10.1073/pnas.85.15.5664

Cited by 84 publications

(37 citation statements)

References 27 publications

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“…B6D2F1 mice (Harlan, Zeist, the Netherlands) were used for Cw3 vaccination. HLA-Cw3 transgenic mice were used as source of antigen-transgenic DCs (13).…”

Section: Methodsmentioning

confidence: 99%

In vivo administration of a lentiviral vaccine targets DCs and induces efficient CD8+ T cell responses

Esslinger¹,

Chapatte²,

Finke³

et al. 2003

J. Clin. Invest.

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“…B6D2F1 mice (Harlan, Zeist, the Netherlands) were used for Cw3 vaccination. HLA-Cw3 transgenic mice were used as source of antigen-transgenic DCs (13).…”

Section: Methodsmentioning

confidence: 99%

In vivo administration of a lentiviral vaccine targets DCs and induces efficient CD8+ T cell responses

Esslinger¹,

Chapatte²,

Finke³

et al. 2003

J. Clin. Invest.

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“…Whether HLA-C molecules are also regularly associated with peptides has not been established (5). Although recognition of HLA-C molecules by alloreactive T cells has been demonstrated (6)(7)(8)(9), very few HLA-C-restricted T cells (10)(11)(12)(13) have been reported; most class I-restricted T cells directed against viral, tumor, or minor histocompatibility antigens are HLA-A or -B restricted. Thus, the function of HLA-C molecules is not well known.…”

mentioning

confidence: 99%

Allele-specific peptide ligand motifs of HLA-C molecules.

Falk

Rötzschke

Grahovac

et al. 1993

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

116

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The consensus motifs of HLA-Cw3, -Cw4, -Cw6, and -Cw7 ligands were determined by pool sequencing. Together with information obtained by sequencing of some prominent individual peptides, the results indicate the following: (t) all four HLA-C molecules are associated with peptides. (i) These peptides adhere to allele-specific motifs that are similar to those of to HLA-A or -B molecules; they have a preferred length of nine amino acids and an anchor residue at the C terminus. (Mi) AU four HLA-C molecules analyzed exhibit related peptide motifs, although each ailelic product shows individual characteristics in fine specificity. (iv) Processing and origin of peptides appear not to be different from that of other class I molecules. (v) No obvious difference at C-terminal position 9 was present in the peptides isolated from the two dimorphic variants of HLA-C that determine dominant resistance to natural killer NKl-speciflc cells (HLA-Cw4, -Cw6) or to NK2-specific cells (HLA-Cw3, -Cw7) and that differ in two residues in or near the pocket at position 9.

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“…With these issues in mind, and because current mouse models are limited in what they can reveal about T cell recognition in the context of the human MHC molecules, we and others have explored the possibility that HLA class I and II molecules expressed in transgenic (Tg) mice might provide a useful model for studying HLA-dependent immune function in vivo (5,(27)(28)(29)(30)(31)(32)(33). For instance, characterization of the non-Tg mouse T cell response to human MHC expressed in tissues of otherwise genetically identical HLA Tg mice (TgM) should make it possible to identify the specific immune mechanisms involved in xeno-MHC recognition and rejection as well as the importance of MHC-dependent vs -independent interactions in the apparent reduced xenogenic cellular response detected in vitro.…”

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confidence: 99%

CD8+ T Cells Are Necessary for Recognition of Allelic, But Not Locus-Mismatched or Xeno-, HLA Class I Transplantation Antigens

Borenstein

Graham

Zhang

et al. 2000

The Journal of Immunology

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Although HLA transgenic mice (HLA TgM) could provide a powerful approach to investigate human MHC-specific T cell responsiveness, the extent to which these molecules are recognized by the mouse immune system remains unclear. We established TgM expressing HLA class I alleles A2, B7, or B27 in their fully native form (HLAnat) or as hybrid molecules (HLAhyb) of the HLA α1/α2 domains linked to the H-2Kb α3, transmembrane, and cytoplasmic domains (i.e., to maintain possible species-specific interactions). Comparison of each as xeno- (i.e., by non-TgM) vs allo- (i.e., by TgM carrying an alternate HLA allele) transplantation Ags revealed the following: 1) Although HLAhyb molecules induced stronger xeno-CD8+ T cell responses in vitro, additional effector mechanisms must be active in vivo because HLAnat skin grafts were rejected faster by non-TgM; 2) gene knockout recipients showed that xenorejection of HLAnat and, unexpectedly, HLAhyb grafts doesn’t depend on CD8+ or CD4+ T cells or B cells; 3) each HLAhyb strain developed tolerance to “self” but rejected allele- (-B27 vs -B7) and locus- (-B vs -A) mismatched grafts, the former requiring CD8+ T cells, the latter by CD8+ T cell-independent mechanisms. The finding that recognition of xeno-HLAhyb does not require CD8+ T cells while recognition of the identical molecule in a strictly allo context does, demonstrates an α1/α2 domain-dependent difference in effector mechanism(s). Furthermore, the CD8+ T cell-independence of locus-mismatched rejection suggests the degree of similarity between self and non-self α1/α2 determines the effector mechanism(s) activated. The HLA Tg model provides a unique approach to characterize these mechanisms and develop tolerance protocols in the context of human transplantation Ags.

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Immunological function of HLA-C antigens in HLA-Cw3 transgenic mice.

Cited by 84 publications

References 27 publications

In vivo administration of a lentiviral vaccine targets DCs and induces efficient CD8+ T cell responses

In vivo administration of a lentiviral vaccine targets DCs and induces efficient CD8+ T cell responses

Allele-specific peptide ligand motifs of HLA-C molecules.

CD8+ T Cells Are Necessary for Recognition of Allelic, But Not Locus-Mismatched or Xeno-, HLA Class I Transplantation Antigens

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