Limunectin. A phosphocholine-binding protein from Limulus amebocytes with adhesion-promoting properties

Abstract

A protein that binds to and precipitates with pneumococcal C-polysaccharide and a phosphocholine (PC) derivative of bovine serum albumin has been affinity purified from Limulus amebocytes. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis reveals that the isolated protein consists of a single polypeptide chain of approximately 50 kDa. It is an intracellular protein localized in the secretory granules of amebocytes according to immunogold staining. Although it shares the PC-binding property with C-reactive protein isolated from Limulus and other animal species, it differs from C-reactive protein in that the latter binds to PC only in the presence of Ca2+, whereas the newly isolated protein binds to PC in a Ca(2+)-independent manner. In this respect, the newly isolated PC-binding protein resembles the antibodies to PC of mouse myelomas. The gene coding for this protein has been isolated. The gene sequence predicts a protein of 54 kDa with an unusual structural feature: it consists almost entirely of 10 contiguous segments, 45 amino acids in length, with extensive homology. Some limited sequence homologies were found between the 54-kDa protein and segments of vitronectin, gelatinase, and collagenase. It binds to bacterial cells, fixed amebocytes, and a number of extracellular matrix molecules. Due to its structural and some functional similarities to other adhesion molecules, the Limulus 54-kDa protein was named "Limunectin."