Key result
Seventy percent of systemic lupus erythematosus sera contained an antibody specificity that cross-reacted with the yeast Sm motif 1 peptide.
Antibodies against a yeast Sm motif 1 peptide cross-react with human Sm core polypeptides, and this cross-reactivity is present in 70% of systemic lupus erythematosus sera.
Hypothesis-generating for molecular mimicry in SLE; does not support clinical interventions based on yeast exposure.
Two regions common to all UsnRNP core polypeptides have been described: Sm motif 1 and Sm motif 2. Rabbits were immunized with a 22 amino-acid peptide containing one segment of Sm motif 1 (YRGTLVSTDNYFNLQLNEAEEF, corresponding to residues 11-32) from yeast F protein. After immunization, the rabbit sera contained antibodies that not only reacted specifically with the peptide from yeast F protein but also cross-reacted with Sm polypeptides from mammals; that is, with purified human U1snRNPs. The results suggest that the peptide used and human Sm polypeptides contain a common feature recognized by the polyclonal antibodies. A large collection of human systemic lupus erythematosus sera was assayed using the yeast peptide as an antigen source. Seventy per cent of systemic lupus erythematosus sera contain an antibody specificity that cross-reacts with the yeast peptide.
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Bahia et al. (1999) studied Systemic lupus erythematosus. Yeast Sm motif 1 peptide was evaluated on Cross-reactivity of SLE sera with yeast Sm motif 1 peptide. Seventy percent of systemic lupus erythematosus sera contained an antibody specificity that cross-reacted with the yeast Sm motif 1 peptide.
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