Evidence of bovine immunoglobulin G1 (IgG1) protease activity in partially purified culture supernate of Pasteurella haemolytica A1.
In the bovine respiratory tract, IgG1 is a major secretory immunoglobulin (Ig), and both IgG1 and IgG2 are believed to be important in defense against pneumonic pasteurellosis (shipping fever) in calves. Here we provide evidence for hydrolysis of IgG1 in the presence of partially purified culture supernate (ppCS) from the respiratory pathogen Pasteurella haemolytica A1. Bovine IgG1 was hydrolysed sequentially into three distinct bands (approximately 39, 12, and 7 kDa respectively). Furthermore, partial hydrolysis of bovine IgG2 was observed, but neither bovine IgA nor IgM were affected by incubation with ppCS. These findings suggest that the production of an IgG1-specific protease by P. haemolytica A1 may be a virulence mechanism contributing to the pathogenesis of bovine pneumonic pasteurellosis.
Lee
C W
CW
Department of Veterinary Microbiology and Immunology, Ontario Veterinary College, University of Guelph.
Shewen
P E
PE
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D015153:Blotting, Western; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D007074:Immunoglobulin G / Q000145:classification / Q000378:metabolism*; D016978:Mannheimia haemolytica / Q000201:enzymology* / Q000276:immunology; D008666:Metalloendopeptidases / Q000378:metabolism*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D007074:Immunoglobulin G; D008666:Metalloendopeptidases; C043859:pseudolysin, Pseudomonas aeruginosa