Two Distinct Types of Aspartic Proteases in the Filarial Parasite Brugia malayi: Molecular Cloning and Tissue Distribution

抄録

The cDNAs coding for two distinct types of aspartic proteases, Bm-ASP-1 and Bm—ASP-2, were cloned from the parasitic nematode Brugia malayi, an important pathogen of human lymphatic filariasis, and their amino acid sequences (393 and 452 residues, respectively, as prepro forms) were deduced. Bm-ASP-1 and Bm-ASP-2 are 29% identical with each other in amino acid sequence and phylogenetic analysis indicated that Bm-ASP-1 and Bm-ASP-2 belong to two different subfamilies of aspartic proteases of nematodes. lmmunohistochemical analysis indicated that Bm-ASP-1 is localized in the intestine and esophagus, while Bm-ASP-2 is distributed more ubiquitously in various tissues including intestine, esophagus, body wall muscle and reproductive system, suggesting their different roles in vivo.