lipid-a has been researched along with Anemia--Hemolytic--Autoimmune* in 2 studies
2 other study(ies) available for lipid-a and Anemia--Hemolytic--Autoimmune
| Article | Year |
|---|---|
Dual recognition of lipid A and DNA by human antibodies encoded by the VH4-21 gene. A possible link between infection and lupus.
Topics: Amino Acid Sequence; Anemia, Hemolytic, Autoimmune; Antibodies, Anti-Idiotypic; Antibodies, Antinuclear; Antibodies, Monoclonal; Antibody Specificity; Antigens, Bacterial; Autoantigens; Autoimmune Diseases; Bacterial Infections; Cross Reactions; DNA; Erythrocytes; Genes, Immunoglobulin; Hemagglutinins; Humans; I Blood-Group System; Immunoglobulin Heavy Chains; Immunoglobulin M; Immunoglobulin Variable Region; Lipid A; Lupus Erythematosus, Systemic; Molecular Mimicry; Molecular Sequence Data; Sequence Alignment; Sequence Homology, Amino Acid | 1995 |
Dual recognition of lipid A and DNA by human antibodies encoded by the VH4-21 gene: a possible link between infection and lupus.
The VH4-21 (V4-34) gene segment, a member of the VH4 family, is expressed early in B-cell maturation and is utilized by approximately 6% of normal adult B lymphocytes. This prevalence indicates an importance of VH4-21 in the B-cell repertoire. The gene also encodes certain autoantibodies being mandatory for pathological IgM anti-red cell antibodies directed against the I/i antigen, and also capable of encoding anti-DNA antibodies. Recognition of I/i antigen or DNA appears to be via two distinct sites on VH, with I/i binding mediated by sequences in the framework region, and DNA binding correlating with the presence of positively charged amino acids in complementarity-determining region 3. However, these positively charged residues appear to suppress the ability of the framework region to interact with I/i, rendering a single sequence monospecific for I/i or DNA. The IgM anti-DNA antibodies also recognize bacterial lipid A, whereas the anti-I/i antibodies do not, indicating that CDR3 may be involved in binding the negatively charged lipid A. Structural similarities between the DNA backbone and lipid A provide a possible explanation for this cross-reactivity. This dual recognition of bacterial antigen and autoantigen provides a potential link between infection and autoimmunity. Topics: Adult; Amino Acid Sequence; Anemia, Hemolytic, Autoimmune; Antibodies, Antinuclear; Antibody Specificity; Antigens, Bacterial; Autoantigens; Cross Reactions; DNA; Genes, Immunoglobulin; Hemagglutination; Humans; Immunoglobulin M; Immunoglobulin Variable Region; Lipid A; Molecular Sequence Data; Sequence Alignment; Structure-Activity Relationship | 1995 |