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. 1995 May;63(5):1703–1709. doi: 10.1128/iai.63.5.1703-1709.1995

Extracellular neuraminidase production by a Pasteurella multocida A:3 strain associated with bovine pneumonia.

D J White 1, W L Jolley 1, C W Purdy 1, D C Straus 1
PMCID: PMC173213  PMID: 7729875

Abstract

The properties of an extracellular neuraminidase produced by a Pasteurella multocida A:3 strain that was isolated in a case of bovine pneumonia were examined during growth in a defined medium. This enzyme (isolated from concentrated culture supernatants of P. multocida A:3) was active against N-acetylneuramin lactose, human alpha-1-acid glycoprotein, fetuin, colominic acid, and bovine submaxillary mucin. Enzyme elaboration was correlated with the growth of the organism in a defined medium, with maximum quantities produced in the stationary phase. The enzyme was purified by a combination of ammonium sulfate fractionation, ion exchange on DEAE-Sephacel, and gel filtration on Sephadex G-200. The purified neuraminidase possessed a specific activity of 9.36 mumol of sialic acid released per min per mg of protein against fetuin. The enzyme possessed a pH optimum of 6.0 and a Km of 0.03 mg/ml. The P. multocida A:3 neuraminidase had a molecular weight of approximately 500,000 as estimated by gel filtration. The enzyme was stable at 4 and 37 degrees C for 3 h. Approximately 75% of the neuraminidase activity was lost within 30 min at 50 degrees C. Greater than 90% of the enzyme activity was destroyed within 10 min at temperatures of > or = 65 degrees C. The P. multocida neuraminidase does not appear to be serologically related to the Pasteurella haemolytica A1 neuraminidase since antiserum prepared against the purified P. haemolytica enzyme did not neutralize the P. multocida enzyme.

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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. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  5. Davis L., Baig M. M., Ayoub E. M. Properties of extracellular neuraminidase produced by group A streptococcus. Infect Immun. 1979 Jun;24(3):780–786. doi: 10.1128/iai.24.3.780-786.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. Rinderknecht H., Geokas M. C., Silverman P., Haverback B. J. A new ultrasensitive method for the determination of proteolytic activity. Clin Chim Acta. 1968 Aug;21(2):197–203. doi: 10.1016/0009-8981(68)90127-7. [DOI] [PubMed] [Google Scholar]
  15. Rutter J. M. Atrophic rhinitis in swine. Adv Vet Sci Comp Med. 1985;29:239–279. [PubMed] [Google Scholar]
  16. 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]
  17. 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]
  18. Straus D. C., Portnoy-Duran C. Neuraminidase production by a Streptococcus sanguis strain associated with subacute bacterial endocarditis. Infect Immun. 1983 Aug;41(2):507–515. doi: 10.1128/iai.41.2.507-515.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Straus D. C., Purdy C. W. In vivo production of neuraminidase by Pasteurella haemolytica A1 in goats after transthoracic challenge. Infect Immun. 1994 Oct;62(10):4675–4678. doi: 10.1128/iai.62.10.4675-4678.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. 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]
  21. 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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