
Antibodies to yeast Sm motif 1 cross‐react with human Sm core polypeptides
Author(s) -
Bahia Diana,
Font Josep,
Khaouja Amina,
Carreras Narcís,
Espuny Ruth,
Cicarelli Regina Maria Barretto,
Ingelmo Miguel,
BachElias Montse
Publication year - 1999
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.1999.00287.x
Subject(s) - polyclonal antibodies , yeast , peptide , antibody , peptide sequence , antigen , microbiology and biotechnology , chemistry , biochemistry , biology , immunology , gene
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.