A V region mutation in a phosphocholine-binding monoclonal antibody results in loss of antigen binding.
A V region mutant producing an antibody that had lost the ability to bind phosphocholine was isolated from a hybridoma producing a germline encoded T15 antibody. The mutation resulted in a single aspartic acid to asparagine substitution at residue 95 of the H chain V region. This confirms that the aspartic acid at residue 95 plays a major role in Ag binding. The results also suggest that somatic cell genetic techniques can be used to generate mAb with useful changes in Ag binding.
Kobrin
B J
BJ
Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461.
Buhl
S
S
Shulman
M J
MJ
Scharff
M D
MD
D000596:Amino Acids / Q000502:physiology; D000818:Animals; D000911:Antibodies, Monoclonal / Q000235:genetics*; D001483:Base Sequence; D007135:Immunoglobulin Variable Region / Q000737:chemistry / Q000235:genetics*; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D009154:Mutation; D010767:Phosphorylcholine / Q000276:immunology*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D000596:Amino Acids; D000911:Antibodies, Monoclonal; D007135:Immunoglobulin Variable Region; D010767:Phosphorylcholine