DOI Seite / Zitierlink:
https://doi.org/10.11588/diglit.48120#0121
Abstracts
103
ly correlated to the primary amino acid sequence indicating that the disease-asso-
ciated epitopes are conformational. As suggested by threedimensional models of
the HLA-molecule, the HVR3 might be involved in the interaction with the T cell
receptor as well as the selected antigenic peptide. To investigate the functional role
of RA-associated T cell epitopes, antigen-specific T cells were established in three
antigenic systems: tetanus toxoid, Epstein-Barr virus and mycobacterial antigens.
Series of antigen-specific T cell clones were generated from DR1+ and DR4 +
RA patients. When these clones were tested for their proliferative response none
of the clones was able to recognize antigen when presented by stimulator cells
similar for the HVR3 but distinct for the HVR2 and HVR1. In a next step
polyclonal T cell lines from DR 1/DR4 heterozygous RA patients were generated.
These lines were either restricted to HLA-DR 1 or DR4 and could not be main-
tained when crosstimulated with the alternative haplotype suggesting that an-
tigen-specific HLA-DR 1 and DR 4 crossreactive T cells are not represented in the
T cell repertoire. These data suggest that the shared conformational T cell
epitopes associated with RA are encoded by a functional domain of the HLA-
molecule which is not involved in selecting an “arthritogenic antigenic peptide”.
The snRNP E Protein: Structure and Expression of a Human
Autoimmune Antigen
E. D. Wieben, D. R. Stanford, M. Fautsch, C. Perry, J. Patton, K. Neiswanger,
E. Holicky, A. Rohleder, R. Sparkes, I. Klisak, B. Knerer, and A. Chang-Miller
Department of Biochemistry and Molecular Biology, Mayo Foundation/Clinic, Rochester,
MN 55905, USA
The snRNP E protein is both an snRNP core protein and a known autoim-
mune antigen. This 10800 dalton basic protein is recognized by a subset of patient
anti-Sm sera. A partial cDNA clone coding for the E protein was originally
isolated from a size-selected cDNA library from HeLa cells. This cDNA clone has
been used as a starting point for investigations of the primary stucture of the pro-
tein, the interaction of this protein with other components of snRNPs, and the
structure and expression of the E protein multigene family.
A full-length cDNA clone isolated from a human teratoma cDNA library has
been fully sequenced. The predicted amino acid sequence from this clone codes
for a basic 92 amino acid polypeptide that contains regions of sequence similarity
to at least one eukaryotic ribosomal protein. Comparison of the primary se-
103
ly correlated to the primary amino acid sequence indicating that the disease-asso-
ciated epitopes are conformational. As suggested by threedimensional models of
the HLA-molecule, the HVR3 might be involved in the interaction with the T cell
receptor as well as the selected antigenic peptide. To investigate the functional role
of RA-associated T cell epitopes, antigen-specific T cells were established in three
antigenic systems: tetanus toxoid, Epstein-Barr virus and mycobacterial antigens.
Series of antigen-specific T cell clones were generated from DR1+ and DR4 +
RA patients. When these clones were tested for their proliferative response none
of the clones was able to recognize antigen when presented by stimulator cells
similar for the HVR3 but distinct for the HVR2 and HVR1. In a next step
polyclonal T cell lines from DR 1/DR4 heterozygous RA patients were generated.
These lines were either restricted to HLA-DR 1 or DR4 and could not be main-
tained when crosstimulated with the alternative haplotype suggesting that an-
tigen-specific HLA-DR 1 and DR 4 crossreactive T cells are not represented in the
T cell repertoire. These data suggest that the shared conformational T cell
epitopes associated with RA are encoded by a functional domain of the HLA-
molecule which is not involved in selecting an “arthritogenic antigenic peptide”.
The snRNP E Protein: Structure and Expression of a Human
Autoimmune Antigen
E. D. Wieben, D. R. Stanford, M. Fautsch, C. Perry, J. Patton, K. Neiswanger,
E. Holicky, A. Rohleder, R. Sparkes, I. Klisak, B. Knerer, and A. Chang-Miller
Department of Biochemistry and Molecular Biology, Mayo Foundation/Clinic, Rochester,
MN 55905, USA
The snRNP E protein is both an snRNP core protein and a known autoim-
mune antigen. This 10800 dalton basic protein is recognized by a subset of patient
anti-Sm sera. A partial cDNA clone coding for the E protein was originally
isolated from a size-selected cDNA library from HeLa cells. This cDNA clone has
been used as a starting point for investigations of the primary stucture of the pro-
tein, the interaction of this protein with other components of snRNPs, and the
structure and expression of the E protein multigene family.
A full-length cDNA clone isolated from a human teratoma cDNA library has
been fully sequenced. The predicted amino acid sequence from this clone codes
for a basic 92 amino acid polypeptide that contains regions of sequence similarity
to at least one eukaryotic ribosomal protein. Comparison of the primary se-