Molecular characterization of a human anti-HIV 1 monoclonal antibody revealed a CD26-related motif in CDR2.
Immunol Lett
; 44(1): 25-30, 1995 Jan.
Article
em En
| MEDLINE
| ID: mdl-7721339
ABSTRACT
Genes encoding the immunoglobulin variable regions of a human anti-HIV-1 IgG1 kappa monoclonal antibody were rescued from a hybridoma, derived from a sero-negative donor, using PCR cloning and expression in Escherichia coli. The ELISA binding results obtained from the expressed Fab fragment confirmed the anti-V3 loop specificity for HIV-1 (LAI) of the original antibody. In addition, an amino acid sequence derived from the second complementarity determining region (CDRH2) of the heavy chain was found to be very similar to the catalytic motif of CD26, a T-cell activation antigen. Furthermore, synthetic peptides containing both the catalytic domain of CD26 and CDRH2 of the antibody showed specific binding to an HIV peptide representing the V3 region in a dose-dependent manner. This suggests an involvement of CD26 as a possible coreceptor for HIV-1.
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Base de dados:
MEDLINE
Assunto principal:
Região Variável de Imunoglobulina
/
Anticorpos Anti-HIV
/
HIV-1
/
Dipeptidil Peptidase 4
/
Anticorpos Monoclonais
Limite:
Humans
Idioma:
En
Ano de publicação:
1995
Tipo de documento:
Article