Antibodies from patients with drug-induced and idiopathic lupus erythematosus react with epitopes restricted to the amino and carboxyl termini of histone.
The sera of patients with systemic lupus erythematosus (SLE) and drug-induced lupus (DIL) were used to study the antigenic epitopes on nuclear histones that bind antibodies in these sera. ELISA and immunoblotting techniques showed that antibodies from both patient groups bound all classes of intact histone: H1 greater than H2B greater than H2A greater than H3 greater than H4. The different classes of histone were enzymatically or chemically cleaved to produce a series of peptide fragments which were then used to map the reactive epitopes by ELISA and immunoblotting. Ten of 11 DIL sera and 11 of 12 SLE sera bound the carboxy and amino terminal peptides. Only one sera of each group bound to the central hydrophobic polypeptide. The reactivity of DIL sera with fractionated histone polypeptides was similar to that observed with SLE sera. This observation suggests that the histone epitopes reacting with DIL sera are no less restricted than those reacting with SLE.
Gohill
J
J
Cary
P D
PD
Couppez
M
M
Fritzler
M J
MJ
D000818:Animals; D001323:Autoantibodies / Q000032:analysis* / Q000145:classification; D001666:Binding Sites, Antibody; D002417:Cattle; D002645:Chickens; D003101:Collodion; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology*; D006657:Histones / Q000145:classification / Q000276:immunology*; D006801:Humans; D008180:Lupus Erythematosus, Systemic / Q000139:chemically induced / Q000276:immunology*; D010209:Paper; D010446:Peptide Fragments / Q000276:immunology*
D001323:Autoantibodies; D000939:Epitopes; D006657:Histones; D010446:Peptide Fragments; D003101:Collodion