Structural properties of a subset of nephritogenic anti-DNA antibodies

Thomas Kieber-Emmons, Mary H. Foster, William V. Williams, Michael P. Madaio

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)172-185
Number of pages14
JournalImmunologic Research
Issue number2-3
StatePublished - Jun 1994


  • Anti-DNA
  • Antibody modeling
  • Autoantibody
  • V gene, variable-region genes

ASJC Scopus subject areas

  • Immunology


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