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Molecular Characterization of the V H 1‐Specific Variable Region Determinants Recognized by Anti‐Idiotypic Monoclonal Antibodies G6 and G8
Author(s) -
Potter,
Qing Li,
Mageed,
Jefferis,
Valérie Capra
Publication year - 1999
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1046/j.1365-3083.1999.00524.x
Subject(s) - idiotopes , idiotype , monoclonal antibody , immunoglobulin idiotypes , antibody , recombinant dna , microbiology and biotechnology , biology , complementarity determining region , gene , monoclonal , virology , genetics
Mutational analysis was used to determine the structural basis for the binding of the murine anti‐idiotypic (anti‐Id) monoclonal antibodies (MoAb) G6 and G8 to V H 1‐encoded antibodies. The MoAb G6 binds a cross‐reactive idiotope present on the heavy (H) chains of immunoglobulins (Ig) encoded by 51p1‐related gene segments, but not those encoded by hv1263‐related gene segments. Gene segments 51p1 (DP‐10) and hv1263 differ by only four amino acids; three in complementarity‐determining region 2 (CDR2), and one in framework region 3 (FR3). The MoAb G8 also binds 51p1‐related sequences, although it is undetermined whether G8 can bind hv1263‐related sequences. In order to localise the Ids recognized by MoAbs G6 and G8 on 51p1‐encoded antibodies, recombinant antibodies containing H‐chain mutants were expressed in insect cells. Idiotypic analysis on the expressed recombinant proteins definitively localised the reactivity in each molecule. These studies should be important in the structural appreciation for critical serological reagents.