Abstract
Autoantibodies against DFS70 (Dense Fine Speckles 70) are found in 30% of Japanese atopic dermatitis patients, and less frequently in patients with other diseases. We have recently reported that they are also seen in 11% of hospital workers, but in only ∼2% of patients with systemic rheumatic disease. In this study, in order to investigate the possible pathological role of anti-DFS70 antibodies, fine epitope mapping was carried out using 93 anti-DFS70 autoantibody-positive sera. Immunoblotting using overlapping peptides failed to reveal major linear epitopes. Western blotting using various truncated proteins showed a strikingly uniform epitope distribution on a suspected tertiary structure expressed by DFS70349-435. Some sera showed reactivity only in an immunoprecipitation assay using an in vitro translated DFS70. Circular dichroism analysis revealed that DFS349-435 contains an approximately 40% alpha-helical conformation, while an overlapping, non-antigenic peptide is composed of random coiled structures. The skewed single major epitope enabled us to establish a highly quantitative ELISA for the epitope region. Antibody titers showed no significant differences between the diseased group and healthy individuals. We propose that anti-DFS70 antibody may be a natural autoantibody, which might modify or reflect the inflammatory process of various disorders.
| Original language | English |
|---|---|
| Pages (from-to) | 221-231 |
| Number of pages | 11 |
| Journal | Journal of Autoimmunity |
| Volume | 23 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 01-01-2004 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Immunology and Allergy
- Immunology
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Autoantigenicity of DFS70 is restricted to the conformational epitope of C-terminal alpha-helical domain. / Ogawa, Yasushi; Sugiura, Kazumitsu; Watanabe, Akihiro; Kunimatsu, Mitoshi; Mishima, Masaki; Tomita, Yasushi; Muro, Yoshinao.
In: Journal of Autoimmunity, Vol. 23, No. 3, 01.01.2004, p. 221-231.Research output: Contribution to journal › Article
TY - JOUR
T1 - Autoantigenicity of DFS70 is restricted to the conformational epitope of C-terminal alpha-helical domain
AU - Ogawa, Yasushi
AU - Sugiura, Kazumitsu
AU - Watanabe, Akihiro
AU - Kunimatsu, Mitoshi
AU - Mishima, Masaki
AU - Tomita, Yasushi
AU - Muro, Yoshinao
PY - 2004/1/1
Y1 - 2004/1/1
N2 - Autoantibodies against DFS70 (Dense Fine Speckles 70) are found in 30% of Japanese atopic dermatitis patients, and less frequently in patients with other diseases. We have recently reported that they are also seen in 11% of hospital workers, but in only ∼2% of patients with systemic rheumatic disease. In this study, in order to investigate the possible pathological role of anti-DFS70 antibodies, fine epitope mapping was carried out using 93 anti-DFS70 autoantibody-positive sera. Immunoblotting using overlapping peptides failed to reveal major linear epitopes. Western blotting using various truncated proteins showed a strikingly uniform epitope distribution on a suspected tertiary structure expressed by DFS70349-435. Some sera showed reactivity only in an immunoprecipitation assay using an in vitro translated DFS70. Circular dichroism analysis revealed that DFS349-435 contains an approximately 40% alpha-helical conformation, while an overlapping, non-antigenic peptide is composed of random coiled structures. The skewed single major epitope enabled us to establish a highly quantitative ELISA for the epitope region. Antibody titers showed no significant differences between the diseased group and healthy individuals. We propose that anti-DFS70 antibody may be a natural autoantibody, which might modify or reflect the inflammatory process of various disorders.
AB - Autoantibodies against DFS70 (Dense Fine Speckles 70) are found in 30% of Japanese atopic dermatitis patients, and less frequently in patients with other diseases. We have recently reported that they are also seen in 11% of hospital workers, but in only ∼2% of patients with systemic rheumatic disease. In this study, in order to investigate the possible pathological role of anti-DFS70 antibodies, fine epitope mapping was carried out using 93 anti-DFS70 autoantibody-positive sera. Immunoblotting using overlapping peptides failed to reveal major linear epitopes. Western blotting using various truncated proteins showed a strikingly uniform epitope distribution on a suspected tertiary structure expressed by DFS70349-435. Some sera showed reactivity only in an immunoprecipitation assay using an in vitro translated DFS70. Circular dichroism analysis revealed that DFS349-435 contains an approximately 40% alpha-helical conformation, while an overlapping, non-antigenic peptide is composed of random coiled structures. The skewed single major epitope enabled us to establish a highly quantitative ELISA for the epitope region. Antibody titers showed no significant differences between the diseased group and healthy individuals. We propose that anti-DFS70 antibody may be a natural autoantibody, which might modify or reflect the inflammatory process of various disorders.
UR - http://www.scopus.com/inward/record.url?scp=14244257153&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=14244257153&partnerID=8YFLogxK
U2 - 10.1016/j.jaut.2004.07.003
DO - 10.1016/j.jaut.2004.07.003
M3 - Article
C2 - 15501393
AN - SCOPUS:14244257153
VL - 23
SP - 221
EP - 231
JO - Journal of Autoimmunity
JF - Journal of Autoimmunity
SN - 0896-8411
IS - 3
ER -