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Pasteurella haemolytica cytotoxin: purification, characterization, and an evaluation of its immunogenicity

Thesis/Dissertation ·
OSTI ID:7108326
The primary goal of the study was to purify P. haemolytica cytotoxin from crude bacterial supernatants. A variety of column chromatographic techniques were evaluated. For each chromatographic procedure factions were evaluated by /sup 51/Cr release assays and enzyme-linked immunosorbent assays (ELISA). Native P. haemolytica cytotoxin is a 160 kilodalton (kDa) protein which is both cytotoxic and immunogenic. With SDS-PAGE it can be degraded into 4 primary proteins of 160, 66, 57, and 23 kDa. The 57 and 66 kDa proteins are antigenic in the bovine as determined by immunoblotting. The ELISA developed for the detection of anticytotoxin antibodies is highly specific for cytotoxic antigens and yields information similar to that obtained by cytotoxin neutralization assays. Cattle with high antibody titers to cytotoxin were found to be better protected against experimental transthoracic exposure to P. haemolytica than were cattle with low titers to cytotoxin. As a predictor of resistance to pneumonic pasteurellosis, cytotoxin ELISA titers were better than titers to somatic antigens.
Research Organization:
Oklahoma State Univ., Stillwater (USA)
OSTI ID:
7108326
Country of Publication:
United States
Language:
English