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Identification of a Novel FcRIIIa-Associated Molecule That Contains Significant Homology to Porcine Cathelin¹

Department of Microbiology and Immunology, Finch University of Health Sciences/Chicago Medical School, North Chicago, IL 60064

The following studies are the first to demonstrate the association of porcine FcRIIIa with a molecule that contains significant homology to the cathelin family of antimicrobial proteins. We performed immunoprecipitation of the porcine FcRIIIa multisubunit complex from Brij 96 lysates of polymorphonuclear leukocytes using the G7 mAb, which binds to FcRIIIa on the surface of porcine NK cells and phagocytes. Previous results indicate that the transmembrane subunit of the FcRIIIa complex is associated with the subunit on the surface of porcine polymorphonuclear leukocytes and with several other unique proteins that surface iodinate and migrate at 15, 20, and 25 kDa when analyzed by reducing SDS-PAGE. Through characterization of the porcine FcRIIIa complex, we identified the 15-kDa molecule as a unique FcR-associated protein that has not been described in other systems. We now report an association between FcRIIIa and a 15-kDa molecule that shares homology to cathelin, a protein of undetermined function initially identified in porcine leukocytes. A domain with a high degree of homology to cathelin is found in the proregions of a family of antibiotic proteins referred to as cathelicidins. The results of our studies indicate the presence of a novel FcRIIIa complex in the porcine system, and may provide new insights into the function of this antimicrobial protein homologue in relation to the variety of responses mediated through FcRs.