Epitope mapping and use of anti-idiotypic antibodies to the L6 monoclonal anticarcinoma antibody

Mouse monoclonal anti-idiotypic antibodies (anti-ids) were raised against L6, a murine IgG2a monoclonal antibody specific for a cell surface antigen expressed by many human carcinomas. Ten distinct anti-ids were generated. Eight anti-ids were shown to inhibit the binding of L6 to its target antigen...

Full description

Saved in:
Bibliographic Details
Published in:Cancer research (Chicago, Ill.) Ill.), 1990-04, Vol.50 (8), p.2449-2454
Main Authors: HELLSTROM, K. E, YELTON, D. E, FELL, H. P, BEATON, D, GAYLE, M, MACLEAN, M, KAHN, M, HELLSTROM, I
Format: Article
Language:English
Subjects:
Animals
Antibodies, Anti-Idiotypic
Antibodies, immunoglobulins
Antibodies, Monoclonal
Antigens, Neoplasm - analysis
Antigens, Surface - analysis
Biological and medical sciences
Cell Line
Chimera
Enzyme-Linked Immunosorbent Assay
Epitopes - analysis
Female
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Humans
Immunoglobulin G
Immunoglobulin Heavy Chains
Immunoglobulin Idiotypes
Immunoglobulin Light Chains
Mice
Mice, Inbred BALB C - immunology
Mice, Inbred C3H - immunology
Molecular immunology
Monoclonal antibodies
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Mouse monoclonal anti-idiotypic antibodies (anti-ids) were raised against L6, a murine IgG2a monoclonal antibody specific for a cell surface antigen expressed by many human carcinomas. Ten distinct anti-ids were generated. Eight anti-ids were shown to inhibit the binding of L6 to its target antigen and were characterized in detail. The heavy and light chain variable region gene segments of the monoclonal antibody L6 linked to human constant regions (chimeric L6) were expressed separately or together, to map the epitopes recognized by the anti-ids. Individual anti-ids were shown to recognize heavy chain, light chain, or combinatorial variable region determinants. Defining these specificities enabled us to select particular anti-ids for assays to monitor the pharmacokinetics of either murine or chimeric L6 antibodies in the circulation of human patients. A quantitative enzyme-linked immunosorbent assay developed with two anti-ids accurately detects less than 5 ng/ml. Anti-ids specific for light chain variable region-encoded determinants were capable of recognizing L6 antigen-binding fragments bound to the surface of human carcinoma cells. These anti-ids can be used to study the binding of chimeric L6 antibody at the surface of tumor cells in histological sections of tumor biopsies.
ISSN:0008-5472
1538-7445