Skip to content
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Menu
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Menu
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
immunology and microbiology
Epitope recognition in histone h1 by sle autoantibodies in the presence of a DNA-ligand
Autoimmunity, Volume 12, No. 3, Year 1992
Notification
URL copied to clipboard!
Description
To investigate the specificity of anti HI antibodies peptides from the N- and C-domain of HI and the synthetic oligonucleotide (AT)6 were complexed. Circular dichroism (CD) spectroscopy indicated that the free peptides H1(1-16), H1(204-218) and C(121-210) in low salt buffer assume a random structure but become helical when bound to the oligonucleotide. The structured and unstructured HI fragments were then analyzed by enzyme linked immunosorbent assay (ELISA) with anti-Hl antibodies in sera from patients with systemic lupus erythematosis (SLE) and with the monoclonal anti-Hl antibody MRA-12 derived from MLR lpr/lpr autoimmune mice. Binding of these antibodies to HI(204-218) and C was inhibited to a level of 50% when these HI peptides were complexed with (AT)6. When the same antibody was tested with HI fragment GC(34-210), attachment to oligonucleotide (AT)6 did not influence antibody binding. Competition studies with liquid phase GC and C antigen against solid phase GC and C indicated that liquid phase GC was more efficient in displacing antibody binding reactivity than liquid phase C. The displacement effect of both liquid phase antigens was greatest against solid phase C. We conclude that anti-Hl autoantibodies are directed against an epitope located near the junction of the G- and C-domain which is exposed and not masked when HI is bound to DNA. © 1992 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
Authors & Co-Authors
Creemers, Pauline C.
South Africa, Cape Town
Stellenbosch University, Faculty of Medicine and Health Sciences
Monestier, Marc
United States, Belleville
Center for Molecular Medicine and Immunology
Böhm, Lothar J.F.
South Africa, Cape Town
Stellenbosch University, Faculty of Medicine and Health Sciences
Statistics
Citations: 4
Authors: 3
Affiliations: 2
Identifiers
Doi:
10.3109/08916939209148456
ISSN:
08916934
Research Areas
Genetics And Genomics