Submitted to: American Society of Microbiologists Abstracts
Publication Type: Abstract Only
Publication Acceptance Date: 5/21/1996
Publication Date: N/A
Technical Abstract: Neuraminidases produced by 16 strains of Pasteurella multocida (serotypes 1 to 16) were characterized by molecular weight, substrate specificity and antigenic identity. After growth in a chemically defined medium, state I (lyophilized) culture supernatants were assayed for activity with N-acetylneuramin lactose, human alpha -1- acid glycoprotein, fetuin, colominic acid, and bovine submaxillary mucin. Neuraminidase produced by P. multocida A:3 (Pm A:3) was purified by a combination of salt fractionation, ion-exchange chromatography on DEAE-Sephacel, and gel filtration on Sephadex G-200. Purified Pm A:3 neuraminidase was employed to immunize rabbits, and the resulting antiserum reduced the activity of the P multocida A:3 enzyme by 40.3%. This antiserum also reduced the activity of the neuraminidases produced by the other serotypes by between 30.8 and 59.6%. Molecular weight estimates of the neuraminidases produced by the various serotypes were obtained by gel filtration chromatography on Sephadex G-200. All 16 serotypes examined produced a neuraminidase with a molecular weight of approximately 500,000. In addition, all sixteen high molecular weight neuraminidases showed similar substrate specificities. On the basis of these data, it appears that the high molecular weight neuraminidases produced by the different P. multocida serotypes are quite similar.