A REFERENCE OF THE GOLD CLASSIFICATION OF MONOCLONAL-ANTIBODIES AGAINST CARCINOEMBRYONIC ANTIGEN TO THE DOMAIN-STRUCTURE OF THE CARCINOEMBRYONIC ANTIGEN MOLECULE
M. Murakami et al., A REFERENCE OF THE GOLD CLASSIFICATION OF MONOCLONAL-ANTIBODIES AGAINST CARCINOEMBRYONIC ANTIGEN TO THE DOMAIN-STRUCTURE OF THE CARCINOEMBRYONIC ANTIGEN MOLECULE, Hybridoma, 14(1), 1995, pp. 19-28
The epitopes of 42 well-characterized monoclonal antibodies (MAbs) aga
inst carcinoembryonic antigen (CEA) from 10 different research groups
were mapped in terms of domain structure (domains N, A1-B1, A2-B2, and
A3-B3) of the CEA molecule on the basis of the reactivities with reco
mbinant CEA proteins expressed in Chinese hamster ovary cells, Thirty-
six of the 42 MAbs tested have previously been classified into 5 essen
tially nonoverlapping epitope groups (GOLD 1-5) by cross-competition a
ssays among MAbs for CEA binding (Hammarstrom S, et al. Cancer Res, 19
89; 49:4852-4858), The epitopes recognized by GOLD 2 MAbs were all pre
sent on domain A2-B2, those for GOLD 5 MAbs were all on domain N, and
those for GOLD 4 were mapped around domains A1-B1 and A2-B2, On the ot
her hand, the epitopes for GOLD 1 MAbs were distributed into domains N
, A2-B2, and A3-B3, and those for GOLD 3 MAbs were separated into doma
ins N and A3-B3, Although the exact reasons for the dispersed patterns
of GOLD 1 and 3 MAbs on the domain structure of the CEA molecule are
unclear at present, several factors, such as a spatial relation or a c
lose proximity of epitopes, conformation dependency, and repetivity of
epitopes, may be considered as possible explanations, The epitope map
ping reported here helps form the basis for understanding the relation
between the chemical structure and antigenic activities of the CEA mo
lecule and may be useful to study the functions of the CEA molecule, e
specially those of the respective domains.