Idioma:

The frequent mutation Gly/Asp in CDR1H may determine a cross‐reactive idiotope in anti‐I cold agglutinins

ABATANGELO, C. ; PLOTKIN, L. ; MATHOV, I. ; SQUIQUERA, L. ; LEONI, J.

Clinical and experimental immunology, 1996-04, Vol.104 (1), p.185-190 [Periódico revisado por pares]

Oxford BSL: Blackwell Science Ltd

Texto completo disponível

Citações Citado por

Enviar para

Título:
The frequent mutation Gly/Asp in CDR1H may determine a cross‐reactive idiotope in anti‐I cold agglutinins
Autor: ABATANGELO, C. ; PLOTKIN, L. ; MATHOV, I. ; SQUIQUERA, L. ; LEONI, J.
Assuntos: Adult ; Agglutinins - chemistry ; Agglutinins - genetics ; Agglutinins - immunology ; Amino Acid Sequence ; Animals ; Antibodies, immunoglobulins ; Antibodies, Monoclonal - immunology ; Aspartic Acid ; autoimmunity ; Biological and medical sciences ; CDR1H ; cold agglutinins ; Cryoglobulins ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Genes, Immunoglobulin ; Genetic markers (allotypes, idiotypes) ; Glycine ; Humans ; Immunoglobulin Heavy Chains - chemistry ; Immunoglobulin Idiotypes - genetics ; Immunoglobulin Variable Region - chemistry ; Mice ; Mice, Inbred BALB C ; Molecular immunology ; Molecular Sequence Data ; Original ; Peptides - immunology ; Point Mutation ; public idiotope ; Solubility ; synthetic peptides
É parte de: Clinical and experimental immunology, 1996-04, Vol.104 (1), p.185-190
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
Descrição: Variable domains (VH) of all known anti i/I cold agglutinin (CA) heavy chains are codified by the VH4–21 gene. While anti‐i CAs are the expression of gene rearrangement without mutations represented by amino acid changes, anti‐I CAs present, among others, a frequent somatic mutation of Gly by Asp at position 31. The hydropathy profile calculated for the CDR1H (position 30 to position 35), as well as some adjacent positions of the heavy chain belonging to anti‐i and anti‐I antibodies, showed the conformational changes accompanying the replacement of Gly by Asp. A MoAb (LP91), which had been obtained in BALB/c mice immunized with a Fabμ fragment from a monoclonal IgMκIIIb anti‐I CA (protein KAU), proved capable of inhibiting human adult erythrocyte cryoagglutination by anti‐I CAs but not that of fetal erythrocytes by anti‐i CAs. Western blot analysis disclosed that such MoAbs recognized a sequential epitope located in the Fd fragment of all anti‐I CAs employed in this study. With the purpose of checking whether Asp31 was involved in the epitope recognized by the MoAb, two peptides, D and G, were synthesized which mimicked the CDR1H structure of anti‐I and anti‐i, respectively; the MoAb only reacted with peptide D by ELISA. Subsequent experimental results indicate that the Gly/Asp mutation could be associated with the diverse specificity presented by these autoantibodies, a change determining a characteristic epitope/idiotope, recognized by LP91 in the CDR1H.
Editor: Oxford BSL: Blackwell Science Ltd
Idioma: Inglês

Links

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

The frequent mutation Gly/Asp in CDR1H may determine a cross‐reactive idiotope in anti‐I cold agglutinins

ABATANGELO, C. ; PLOTKIN, L. ; MATHOV, I. ; SQUIQUERA, L. ; LEONI, J.

Oxford BSL: Blackwell Science Ltd

Buscando em bases de dados remotas. Favor aguardar.