Proteolytic cleavage of IgG and other protein substrates by Dirofilaria immitis microfilarial enzymes.
Proteases were detected in aqueous extracts of Dirofilaria immitis microfilariae. Enzymes within the extract were capable of hydrolyzing Azocoll, a general protease substrate, at pH's 7, 8, and 9. Sensitivities to a variety of protease inhibitors indicated that multiple azocollytic enzymes were present in the extract, most prominent of which appear to belong to the serine class of proteases. By incorporating various substrates into the matrices of polyacrylamide gels, 2 SDS-resistant, mercaptoethanol-sensitive proteases in the MF extract were identified at 22 and 76 kDa. These proteases showed differential abilities to digest casein, fibrinogen, hemoglobin, and IgG. The MF extract hydrolyzed radiolabeled IgG into 8-10-kDa fragments following a 20-hr incubation. A similar degree of digestion was observed in 2 hr when viable microfilariae were used. The potential significance of these proteases in the evasion of host effector mechanisms is discussed.
D000818:Animals; D004049:Diethylcarbamazine / Q000494:pharmacology; D004183:Dirofilaria immitis / Q000201:enzymology*; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000378:metabolism; D005370:Filarioidea / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007074:Immunoglobulin G / Q000378:metabolism*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000032:analysis*
D007074:Immunoglobulin G; D005340:Fibrinogen; D010447:Peptide Hydrolases; D004049:Diethylcarbamazine