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Department of Physiology and Biochemistry, University of Veterinary Science, Budapest, Hungary;
Rosenstiel Center for Basic Biomedical Sciences, W. M. Keck Institute for Cellular Visualization, and Biology Department, Brandeis University, Waltham, MA 02254; and
Center for Biotechnology, Karolinska Institute, Stockholm, Sweden
In the cow, maternal immunity is exclusively mediated by colostral
Igs, but the receptor responsible for the IgG transport has not yet
been identified. The role of an IgG-Fc receptor (FcRn) that resembles a
class I MHC Ag in transporting IgGs through epithelial cells was
recently shown in selected species. We now report the cloning and
characterization of the bovine FcRn (bFcRn). The cDNA and deduced amino
acid sequences show high similarity to the FcRn in other species, and
it consists of three extracellular domains, a hydrophobic transmembrane
region, and a cytoplasmic tail. Despite the high similarity of the
extracellular domains with other species, the bovine cytoplasmic tail
is the shortest thus far analyzed. Aligning the known FcRn sequences,
we noted that the bovine protein shows a 3-aa deletion compared to the
rat and mouse sequences in the 
1 loop. Furthermore, we found a
shorter transcript of the bFcRn reflecting an exon 6-deleted mRNA,
which results from an inadequate splice acceptor site in intron 5 and
produces a transmembrane-deficient molecule, as was previously
demonstrated in the related MHC class I gene family in mouse and
humans. The presence of bFcRn transcripts in multiple tissues,
including the mammary gland, suggests their involvement both in IgG
catabolism and transcytosis.
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