Characterization of neuraminidases produced by various serotypes of Pasteurella multocida.

Infection and Immunity
D C StrausC W Purdy

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, stage 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 was purified by a combination of salt fractionation, ion-exchange chromatography on DEAE-Sephacel, and gel filtration on Sephadex G-200. Purified P. multocida 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 activities of the neuraminidases produced by 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. Each of the 16 serotypes examined produced a neuraminidase with a molecular weight of approximately 500,000. In addition, all 16 high-molecular-weight neuraminidases showed similar substrate specificities. On the basis of these dat...Continue Reading

References

Mar 1, 1977·Journal of Bacteriology·M FlashnerS W Tanenbaum
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Citations

Jul 8, 2000·Letters in Applied Microbiology·H SugitaR Okano
May 17, 2008·Avian Pathology : Journal of the W.V.P.A·J P Christensen, M Bisgaard
Jul 15, 1997·FEMS Microbiology Letters·C A Lichtensteiger, E R Vimr

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