The structure of bovine secretory component

Bovine secretory component (SC) has been cleaved with trypsin into a series of fragments and their N-terminal amino acid sequences have been determined. The close homology with the known sequence of human SC has enabled the sequential order of the fragments to be deduced. The results indicate that bovine SC consists of a single glycosylated polypeptide chain (Mr 74,000) folded into five globular immunoglobulin-like domains. A protein (Mr 94,000) has been isolated from detergent solubilised bovine epithelial membranes from liver, intestine and mammary gland. This membrane protein is specific for the binding of J-chain linked IgM and IgA dimers. It can be proteolytically cleaved into a water soluble SC-like portion and a detergent soluble hydrophobic portion. Bovine SC is therefore most likely to be the extracellular part of an epithelial receptor which mediates the transport of IgA dimers to mucosal surfaces. The various tryptic fragments from bovine SC have been shown to differ in their relative binding affinities for IgM and IgA dimers. The results imply that the first three domains of bovine SC are most involved in binding and domains 4 and 5 play subsidiary roles. Computerized prediction and modelling methods have been used to deduce possible tertiary and quaternary structures for SC. There are good indications that the molecule has an elonaged "zig-zag" structure stabilized by longitudinal inter-domain contacts. A model of SC bound to IgA dimer is presented.