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SNRPD1  -  small nuclear ribonucleoprotein D1...

Homo sapiens

Synonyms: HsT2456, SMD1, SNRPD, Sm-D autoantigen, Sm-D1, ...
 
 
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Disease relevance of SNRPD1

  • Sm-D1 is a component of small nuclear ribonucleoprotein (snRNP) complexes which are associated with autoimmune disease [1].
  • Because the BB'Sm proteins share cross-reactive epitopes (PPPGMRPP) with U1 specific ribonucleoproteins, which are more frequently targeted by antibodies that are present in patients with mixed connective tissue disease, the SmD polypeptides are regarded as the Sm autoantigens that are most specific to SLE [2].
  • These A3 immunized rabbits also develop antibodies to common antigenic regions of nRNP 70K, nRNP C, Sm B/B', and Sm D1 proteins, as well as clinical symptoms of systemic lupus erythematosus such as leukopenia and renal insufficiency [3].
  • OBJECTIVE: To characterize the 15-kd human SmD-like autoantigen and its associated proteins previously shown to be recognized by IgM antibodies in patients with Epstein-Barr virus (EBV)-induced infectious mononucleosis [4].
  • We isolated and characterized the antibodies present in lupus sera that are specific for the C-terminal region of SmD (sequence 95-119) [5].
 

High impact information on SNRPD1

  • The U7 snRNP involved in histone RNA 3' processing contains a structurally similar but biochemically unique Sm core in which two of these proteins, Sm D1 and D2, are replaced by Lsm10 and by another as yet unknown component [6].
  • We show that SMN binds preferentially to the dimethylarginine-modified RG domains of SmD1 and SmD3 [7].
  • JBP1 binds SmD1 and SmD3 via their RG domains, while pICln binds the Sm domains [8].
  • T cell epitopes on SmD were mapped in A/J mice and were localized to three regions on SmD, within aa 26-55, 52-69, and 86-115 [9].
  • In addition, the sera did not react with other regions on SmD, indicating a lack of intramolecular B cell epitope spreading within SmD [9].
 

Biological context of SNRPD1

  • The third gene, termed SNRPD1, shares 100% identity to the cDNA sequence including both 5'- and 3'-untranslated regions (UTR); it contains three introns [10].
  • One of the D3 epitopes (RGRGRGMGR) has significant sequence homology with a major antigenic region of Sm D1 (containing a carboxyl-terminal glycine-arginine repeat), and anti-D3 Abs cross-react with this epitope of Sm D1 [11].
  • Southern blotting and DNA sequencing analysis of these clones revealed the presence of an Sm-D1 multigene family in the human genome [10].
  • The SmB, SmD1, and SmD3 proteins have the rare symmetrical dimethylarginine post-translational modification in their C-termini [12].
  • A SmD Peptide Induces Better Antibody Responses to Other Proteins within the Small Nuclear Ribonucleoprotein Complex than to SmD Protein via Intermolecular Epitope Spreading [9].
 

Anatomical context of SNRPD1

  • However, only SmD(52-66) immunization induced T cells capable of reacting with SmD [9].
  • Antibodies against U1A (tested in Western immunoblotting with HeLa cell extracts) were positively associated to DRB1*06 allele; antibodies reacting with SmD1 peptide 44-67 were negatively associated to DRB1*02 and DQB1*0602 alleles [13].
 

Associations of SNRPD1 with chemical compounds

  • Using immobilized peptides, we confirmed that the dimethylated arginine residues play an essential role in the formation of major SmD1 and SmD3 autoepitopes [2].
 

Other interactions of SNRPD1

 

Analytical, diagnostic and therapeutic context of SNRPD1

  • Molecular cloning of a cDNA encoding the human Sm-D autoantigen [15].
  • Using the yeast two hybrid assay, we identified Sm-D1, a host protein that binds to NS3 [1].
  • The high sensitivity of this ELISA probably depends on a conformational epitope, which appears not to be accessible in the full-size SmD1 protein [16].
  • However, in comparison with the authentic protein, the recombinant hSm-D1 displayed different immunoreactive determinants as assessed by Western blot [14].
  • Immunoprecipitation of in vitro translated deletion mutants of both Sm-B and Sm-D1 was also employed to determine the sequence requirements for recognition by two monoclonal antibodies that are cross-reactive with several Sm proteins, Y12 and ANA128 [17].

References

  1. Hepatitis C virus nonstructural protein NS3 binds to Sm-D1, a small nuclear ribonucleoprotein associated with autoimmune disease. Iwai, A., Hasumura, Y., Nojima, T., Takegami, T. Microbiol. Immunol. (2003) [Pubmed]
  2. Identification of a SmD3 epitope with a single symmetrical dimethylation of an arginine residue as a specific target of a subpopulation of anti-Sm antibodies. Mahler, M., Fritzler, M.J., Blüthner, M. Arthritis Res. Ther. (2005) [Pubmed]
  3. Structural availability influences the capacity of autoantigenic epitopes to induce a widespread lupus-like autoimmune response. McClain, M.T., Lutz, C.S., Kaufman, K.M., Faig, O.Z., Gross, T.F., James, J.A. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  4. Autoantibody to hLSm4 and the heptameric LSm complex in anti-Sm sera. Eystathioy, T., Peebles, C.L., Hamel, J.C., Vaughn, J.H., Chan, E.K. Arthritis Rheum. (2002) [Pubmed]
  5. Autoantibodies from patients with systemic lupus erythematosus bind a shared sequence of SmD and Epstein-Barr virus-encoded nuclear antigen EBNA I. Sabbatini, A., Bombardieri, S., Migliorini, P. Eur. J. Immunol. (1993) [Pubmed]
  6. Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing. Pillai, R.S., Grimmler, M., Meister, G., Will, C.L., Lührmann, R., Fischer, U., Schümperli, D. Genes Dev. (2003) [Pubmed]
  7. SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Friesen, W.J., Massenet, S., Paushkin, S., Wyce, A., Dreyfuss, G. Mol. Cell (2001) [Pubmed]
  8. The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins. Friesen, W.J., Paushkin, S., Wyce, A., Massenet, S., Pesiridis, G.S., Van Duyne, G., Rappsilber, J., Mann, M., Dreyfuss, G. Mol. Cell. Biol. (2001) [Pubmed]
  9. A SmD Peptide Induces Better Antibody Responses to Other Proteins within the Small Nuclear Ribonucleoprotein Complex than to SmD Protein via Intermolecular Epitope Spreading. Deshmukh, U.S., Bagavant, H., Sim, D., Pidiyar, V., Fu, S.M. J. Immunol. (2007) [Pubmed]
  10. Analysis of genes for human snRNP Sm-D1 protein and identification of the promoter sequence which shows segmental homology to the promoters of Sm-E and U1 snRNA genes. Sun, D., Ou, Y.C., Hoch, S.O. Gene (1997) [Pubmed]
  11. Anti-sm autoantibodies in systemic lupus target highly basic surface structures of complexed spliceosomal autoantigens. McClain, M.T., Ramsland, P.A., Kaufman, K.M., James, J.A. J. Immunol. (2002) [Pubmed]
  12. The symmetrical dimethylarginine post-translational modification of the SmD3 protein is not required for snRNP assembly and nuclear transport. Khusial, P.R., Vaidya, K., Zieve, G.W. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  13. MHC class II gene associations with autoantibodies to U1A and SmD1 proteins. Dumortier, H., Abbal, M., Fort, M., Briand, J.P., Cantagrel, A., Muller, S. Int. Immunol. (1999) [Pubmed]
  14. Overproduction of a human snRNP-associated Sm-D autoantigen in Escherichia coli and Saccharomyces cerevisiae. Rokeach, L.A., Haselby, J.A., Hoch, S.O. Gene (1992) [Pubmed]
  15. Molecular cloning of a cDNA encoding the human Sm-D autoantigen. Rokeach, L.A., Haselby, J.A., Hoch, S.O. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  16. A novel epitope on the C-terminus of SmD1 is recognized by the majority of sera from patients with systemic lupus erythematosus. Riemekasten, G., Marell, J., Trebeljahr, G., Klein, R., Hausdorf, G., Häupl, T., Schneider-Mergener, J., Burmester, G.R., Hiepe, F. J. Clin. Invest. (1998) [Pubmed]
  17. Mapping of SLE-specific Sm B cell epitopes using murine monoclonal antibodies. Pruijn, G.J., Schoute, F., Thijssen, J.P., Smeenk, R.J., van Venrooij, W.J. J. Autoimmun. (1997) [Pubmed]
 
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