Antibodies to B7.1 define the GFCC'C" face of the N-terminal domain as critical for co-stimulatory interactions.
Antagonists of the B7 family of co-stimulatory molecules have the potential for altering immune responses therapeutically. To better define the requirements for such inhibitors, we have mapped the binding of an entire panel of blocking antibodies specific for human B7.1. By mutagenesis, each of the residues critical for blocking antibody binding appeared to fall entirely within the N-terminal V-set domain of B7.1. Thus, although antibody-antigen interacting surfaces can be quite large, these results indicate that a relatively small portion of the GFCC'C" face of this domain is crucial for further antagonist development.
Wang
Suyue
S
Wyeth Research, 200 Cambridge Park Drive, MA 02140, USA.
Veldman
Geertruida M
GM
Stahl
Mark
M
Xing
Yuzhe
Y
Tobin
James F
JF
Erbe
David V
DV
D000595:Amino Acid Sequence; D000818:Animals; D019138:Antibodies, Blocking / Q000235:genetics / Q000276:immunology; D018122:B7-1 Antigen / Q000235:genetics / Q000276:immunology*; D019556:COS Cells; D018604:Epitope Mapping; D018985:Epitopes, B-Lymphocyte; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000235:genetics / Q000276:immunology; D051379:Mice; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000276:immunology
D019138:Antibodies, Blocking; D018122:B7-1 Antigen; D018985:Epitopes, B-Lymphocyte; D007141:Immunoglobulin Fc Fragments; D011993:Recombinant Fusion Proteins