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Brief Definitive Report |
Address correspondence to Dr. J. Donald Capra, Oklahoma Medical Research Foundation, 825 N.E. 13th St., Oklahoma City, OK 73104. Phone: 405-271-7210; Fax: 405-271-8237; E-mail: Jdonald-Capra{at}omrf.ouhsc.edu
Polymeric immunoglobulins provide first line humoral defense at mucosal surfaces to which they are specifically transported by the polymeric immunoglobulin receptor (pIgR) on mucosal and glandular epithelial cells. Previous studies from our laboratory suggested that amino acids 402–410 of the C
3 domain of dimeric IgA (dIgA) represented a potential binding site for the pIgR. Here by binding human secretory component to overlapping decapeptides of C3, we confirm these residues and also uncover an additional site. Furthermore, we show that the C3 motif appears to be sufficient to direct transport of green fluorescent protein through the pIgR-specific cellular transcytosis system. An alternative approach identified phage peptides, selected from a library by the in vitro Madin Darby Canine Kidney transcytosis assay, for pIgR-mediated transport through epithelial cells. Some transcytosis-selected peptides map to the same 402–410 pIgR-binding C3 site. Further in vivo studies document that at least one of these peptides is transported in a rat model measuring hepatic bile transport. In addition to identifying small peptides that are both bound and transported by the pIgR, this study provides evidence that the pIgR-mediated mucosal secretion system may represent a means of targeting small molecule therapeutics and genes to mucosal epithelial cells.
Key Words: mucosal immunity • IgA • transcytosis • secretory IgA • phage display library
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