Purification
and Partial Sequencing of the Fc Region of Immunoglobulin G from the
Atlantic Bottlenose Dolphin, Tursiops
truncatus
Kathleen
E. Kohlberg, M.S.
Grice
Marine Laboratory, University
of Charleston
Department
of Microbiology and Immunology, Medical University of South Carolina
ABSTRACT
Despite much popular interest in marine mammals, the structural and functional
characteristics of cetacean immunoglobulins have not been widely reported. The
present study focused on the purification and characterization of IgG Fc region
from the Atlantic bottlenose dolphin, Tursiops truncatus. In mammals, the
ability of an antibody to recruit functional activity of the innate immune
system is based on its Fc region. IgG was isolated from dolphin sera by FPLC on
Protein G Sepharose and digested with papain. The partial amino acid sequence of
the Fc region was obtained and compared to those of artiodactyls (even-toed
ungulates). The partial Fc region of dolphin IgG was highly similar to the
corresponding regions of ruminant IgG, but differed greatly from the same region
of suiform IgG. This represents the first reported isolation and sequencing of a
cetacean immunoglobulin Fc region. These data should be useful not only for
developing probes to evaluate the dolphin immune response to pathogens and
contaminants in their environment, but also to encourage further detailed
studies of the dolphin antibody repertoire.