Nuclear antigens of Schistosoma mansoni revealed by sera from systemic autoimmune diseases

作者：Caride EC; Tempone AJ; Rumjanek FD^*

来源：Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology, 1997, 118(4): 797-803.

DOI：10.1016/S0305-0491(97)00239-3

• autoantibodies
• immunoaffinity
• nuclear proteins
• autoimmune
• disease
• ribosomal
• RNA
• Schistosoma mansoni
• transcription

Nuclear proteins from Schistosoma mansoni were extracted, fractionated and screened with sera from 178 individuals suffering from rheumatoid arthritis (RA) and systemic lupus erythematosus (SLE). Only chose individuals residing in non endemic areas for schistosomiasis were selected for this study. Reference sera recognizing specific ribonucleoproteins and DNA were also included. The aim was to use the autoantibodies as probes co identify potential transcription factors in S. mansoni. Immunoblot assays with sera from RA and SLE individuals yielded complex patterns that could nevertheless be distinguished from each other. Immunoaffinity chromatography using immobilized immunoglobulins obtained from pools of these two groups was carried out to purify I-125-labeled and unlabeled S. mansoni nuclear proteins. The results showed that the IgGs from SLE bound to proteins with a molecular weight of similar to 31 kDa, not recognized by RA immunoglobulins. Most SLE sera and some RA sera recognized a major S. mansoni nuclear protein that had been previously characterized as a high mobility group protein. Among the reference sera, the anti-double-stranded DNA, anti-U1 RNP, anti-Sm and anti-DNA topoisomerase all reacted with the schistosome extract, yielding major bands for each serum. Using the super shift technique, it was shown that the 31-kDa proteins interacted with the upstream domain of the ribosomal RNA gene of S. mansoni.

• 出版日期1997-12