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. 1996 Apr;64(4):1446–1449. doi: 10.1128/iai.64.4.1446-1449.1996

Characterization of neuraminidases produced by various serotypes of Pasteurella multocida.

D C Straus 1, W L Jolley 1, C W Purdy 1
PMCID: PMC173941  PMID: 8606116

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 data, it appears that the high-molecular-weight neuraminidases produced by different P. multocida serotypes are quite similar.

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Selected References

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  1. AMINOFF D. Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochem J. 1961 Nov;81:384–392. doi: 10.1042/bj0810384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Balke E., Scharmann W., Drzeniek R. Die Bestimmung des Molekulargewichtes bakterieller Neuraminidasen mit Hilfe der Gel-Filtration. Zentralbl Bakteriol Orig A. 1974;229(1):55–67. [PubMed] [Google Scholar]
  3. Carter G. R. Pasteurellosis: Pasteurella multocida and Pasteurella hemolytica. Adv Vet Sci. 1967;11:321–379. [PubMed] [Google Scholar]
  4. Confer A. W. Immunogens of Pasteurella. Vet Microbiol. 1993 Nov;37(3-4):353–368. doi: 10.1016/0378-1135(93)90034-5. [DOI] [PubMed] [Google Scholar]
  5. Drzeniek R., Scharmann W., Balke E. Neuraminidase and N-acetylneuraminate pyruvate-lyase of Pasteurella multocida. J Gen Microbiol. 1972 Sep;72(2):357–368. doi: 10.1099/00221287-72-2-357. [DOI] [PubMed] [Google Scholar]
  6. Drzeniek R. Viral and bacterial neuraminidases. Curr Top Microbiol Immunol. 1972;59:35–74. doi: 10.1007/978-3-642-65444-2_2. [DOI] [PubMed] [Google Scholar]
  7. Flashner M., Wang P., Hurley J. B., Tanenbaum S. W. Properties of an inducible extracellular neuraminidase from an Arthrobacter isolate. J Bacteriol. 1977 Mar;129(3):1457–1465. doi: 10.1128/jb.129.3.1457-1465.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HUGHES R. C., JEANLOZ R. W. THE EXTRACELLULAR GLYCOSIDASES OF DIPLOCOCCUS PNEUMONIAE. I. PURIFICATION AND PROPERTIES OF A NEURAMINIDASE AND A BETA-GALACTOSIDASE. ACTION ON THE ALPHA-1-ACID GLYCOPROTEIN OF HUMAN PLASMA. Biochemistry. 1964 Oct;3:1535–1543. doi: 10.1021/bi00898a025. [DOI] [PubMed] [Google Scholar]
  9. Ifeanyi F. I., Bailie W. E. Passive protection of mice with antiserum to neuraminidase from Pasteurella multocida serotype A:3. Vet Res Commun. 1992;16(2):97–105. doi: 10.1007/BF01839006. [DOI] [PubMed] [Google Scholar]
  10. Kelly R. T., Greiff D., Farmer S. Neuraminidase activity in Diplococcus pneumoniae. J Bacteriol. 1966 Feb;91(2):601–603. doi: 10.1128/jb.91.2.601-603.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Manning P. J. Naturally occurring pasteurellosis in laboratory rabbits: chemical and serological studies of whole cells and lipopolysaccharides of Pasteurella multocida. Infect Immun. 1984 May;44(2):502–507. doi: 10.1128/iai.44.2.502-507.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Moriyama T., Barksdale L. Neuraminidase of Corynebacterium diphtheriae. J Bacteriol. 1967 Nov;94(5):1565–1581. doi: 10.1128/jb.94.5.1565-1581.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Müller H. E., Krasemann C. Die Virulenz von Pasteurella multocida-Stämmen und ihre Neuraminidase-Produktion. Zentralbl Bakteriol Orig A. 1974;229(3):391–400. [PubMed] [Google Scholar]
  15. Müller H. E. Untersuchungen in vitro über di Neuraminidase der Pasteurella multocida. Zentralbl Bakteriol Orig A. 1971 Jul;217(3):326–344. [PubMed] [Google Scholar]
  16. Müller H. E. Unterushungen über die in vivo-Wirkung von Neuraminidase bei Pasteurella multocida. Z Immunitatsforsch Exp Klin Immunol. 1971 Jul;142(1):31–37. [PubMed] [Google Scholar]
  17. Rimler R. B. Comparisons of Pasteurella multocida lipopolysaccharides by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to determine relationship between group B and E hemorrhagic septicemia strains and serologically related group A strains. J Clin Microbiol. 1990 Apr;28(4):654–659. doi: 10.1128/jcm.28.4.654-659.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Rutter J. M. Atrophic rhinitis in swine. Adv Vet Sci Comp Med. 1985;29:239–279. [PubMed] [Google Scholar]
  19. Scharmann W., Drzeniek R., Blobel H. Neuraminidase of Pasteurella multocida. Infect Immun. 1970 Mar;1(3):319–320. doi: 10.1128/iai.1.3.319-320.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Straus D. C., Jolley W. L., Purdy C. W. Characterization of neuraminidases produced by various serotypes of Pasteurella haemolytica. Infect Immun. 1993 Nov;61(11):4669–4674. doi: 10.1128/iai.61.11.4669-4674.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Straus D. C., Purdy C. W. Extracellular neuraminidase production by Pasteurella species isolated from infected animals. Curr Microbiol. 1995 Nov;31(5):312–315. doi: 10.1007/BF00314586. [DOI] [PubMed] [Google Scholar]
  22. Straus D. C., Unbehagen P. J., Purdy C. W. Neuraminidase production by a Pasteurella haemolytica A1 strain associated with bovine pneumonia. Infect Immun. 1993 Jan;61(1):253–259. doi: 10.1128/iai.61.1.253-259.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. White D. J., Jolley W. L., Purdy C. W., Straus D. C. Extracellular neuraminidase production by a Pasteurella multocida A:3 strain associated with bovine pneumonia. Infect Immun. 1995 May;63(5):1703–1709. doi: 10.1128/iai.63.5.1703-1709.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Wijewardana T. G., Wilson C. F., Gilmour N. J., Poxton I. R. Production of mouse monoclonal antibodies to Pasteurella multocida type A and the immunological properties of a protective anti-lipopolysaccharide antibody. J Med Microbiol. 1990 Dec;33(4):217–222. doi: 10.1099/00222615-33-4-217. [DOI] [PubMed] [Google Scholar]

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