Structural properties of a subset of nephritogenic anti-DNA antibodies.
Structural analysis of lupus autoantibodies is beginning to provide clues to the molecular basis for antigenic specificity and pathogenicity. The present analysis indicates that multiple light and heavy chains contain residues which can facilitate DNA binding, reaffirming the notion that there are multiple ways that different amino acids combine to form an antigen-binding pocket with affinity for dsDNA and ssDNA. Furthermore, this analysis suggests that these conformations and contact residues are intrinsic to germline sequences, although amino acid changes at critical locations (somatically introduced) modulate antigen binding, and appear to influence the capacity of individual immunoglobulin to form immune deposits. Analysis of additional individual immunoglobulins with closely related V-region sequences and differing pathogenic properties will be required to resolve the contribution of specific motifs to pathogenecity.
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Related Subject Headings
- Molecular Sequence Data
- Models, Molecular
- Immunology
- Immunoglobulin Variable Region
- Immunoglobulin Light Chains
- Immunoglobulin Heavy Chains
- Humans
- Glomerulonephritis
- Antibodies, Monoclonal
- Antibodies, Antinuclear
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Molecular Sequence Data
- Models, Molecular
- Immunology
- Immunoglobulin Variable Region
- Immunoglobulin Light Chains
- Immunoglobulin Heavy Chains
- Humans
- Glomerulonephritis
- Antibodies, Monoclonal
- Antibodies, Antinuclear