Disease relevance of Igkv4-71

• Immunization with the light chain and the VL domain of the isologous myeloma protein 315 inhibits growth of mouse plasmacytoma MOPC315 [1].
• Expression of the VL-domain of mouse monoclonal antibody F11 to human spleen ferritin in Escherichia coli cells is associated with the formation of insoluble protein aggregates (inclusion bodies) [2].

High impact information on Igkv4-71

• Isolated variable region light chain 315 (VL-315), the VL domain of a myeloma protein of BALB/c origin, induces T cells of BALB/c (H-2d) mice that help the adoptive secondary anti-4-hydroxy-3-iodo-5-nitrophenylacetyl (NIP) antibody response to NIP-Fab315 [3].
• Those with 5- and 15-residue linkers had similar binding affinities to the parent antibodies, but a fragment with the VH domain joined directly to the VL domain was found to have slower dissociation kinetics and an improved affinity for hapten [4].
• Thus, the isolation and expression of VH and VL domain genes are of particular interest both for analysis of the determinants of antibody specificity and for generation of fragments with binding affinities for use in therapy and diagnosis [5].
• Significant differences between the VL domain dimer and the Fab fragment in the third complementarity-determining region show that knowledge of the structure of the dimerization partner and its exact mode of association may be needed to predict the precise conformation of antigen-binding loops [6].
• The VL domain alone did not bind to nucleic acids, but VL association modified the VH binding, giving the scFv a 10-fold higher affinity than the VH for poly(dC) and greatly increasing the cytosine-dependent selectivity [7].

Biological context of Igkv4-71

• Bacteria were engineered for the expression of mouse immunoglobulin light chain variable region (VL) and heavy chain variable region (VH) fusion proteins. cDNAs encoding the VL and VH of anti-alpha(1----6)dextran hybridoma protein 19.22.1 were inserted into the pATH 10 prokaryotic expression vector downstream of trp operon sequences [8].

Anatomical context of Igkv4-71

• T helper lymphocytes recognize the VL domain of the isologous mouse myeloma protein 315 [9].

Associations of Igkv4-71 with chemical compounds

• The aggregates were solubilized in the presence of guanidine hydrochloride and the recombinant VL-domain was purified by immobilized metal affinity chromatography (IMAC) [2].

Analytical, diagnostic and therapeutic context of Igkv4-71

• Additional data from competitive inhibition assays with isolated and recombined H and L chains from a prototype monoclonal anti-GAC antibody (HGAC 39), and from isoelectric focusing of whole or reduced and alkylated HGAC 39, suggested that one of the idiotopes was located, at least primarily, on the VL domain [10].
• Functional activity of the VL-domain was verified by two variants of ELISA [2].
• The data indicate that the recombinant VL-domain can be used in construction of chimeric immunotoxins and other antigen-binding proteins in immunotherapy and in studies of correlations between folding, stability, and activity of immunoglobulins [2].

References