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. 1965 May;89(5):1217–1224. doi: 10.1128/jb.89.5.1217-1224.1965

Preparation and Properties of a Vi Antigen-Degrading Enzyme

Edgar E Baker 1, Roberta E Whiteside 1
PMCID: PMC277631  PMID: 14292989

Abstract

Baker, Edgar E. (Boston University School of Medicine, Boston, Mass.), and Roberta E. Whiteside. Preparation and properties of a Vi antigen-degrading enzyme. J. Bacteriol. 89:1217–1224. 1965.—Vi antigen can be hydrolyzed by an inducible enzyme produced by a microorganism isolated from soil. The organism can be identified as Bacillus sphaericus. The enzyme in the culture supernatant fluid can be concentrated and partially purified by precipitation with ammonium sulfate at 50% of saturation. The partially purified enzyme is relatively stable. Incubation of the enzyme with Vi antigen causes a rapid loss of serological activity, a decrease in viscosity, the loss of ability to precipitate albumin at pH 4.0, and the production of reducing sugar and hexosamine. Optimal conditions for enzyme action on Vi antigen are pH 8.4 and 40 C. The reaction rate is independent of the substrate concentration. Intact protein and calcium activates the Vi antigen-enzyme system. The enzyme is not inhibited by its reaction products.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BAKER E. E., WHITESIDE R. E., BASCH R., DEROW M. A. The VI antigens of the Enterobacteriaceae. I. Purification and chemical properties. J Immunol. 1959 Dec;83:680–696. [PubMed] [Google Scholar]
  2. CLARK W. R., McLAUGHLIN J., WEBSTER M. E. An aminohexuronic acid as the principal hydrolytic component of the Vi antigen. J Biol Chem. 1958 Jan;230(1):81–89. [PubMed] [Google Scholar]
  3. Chase M. W. A Microorganism Decomposing Group-Specific A Substances. J Bacteriol. 1938 Oct;36(4):383–390. doi: 10.1128/jb.36.4.383-390.1938. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. GADEBUSCH H. H., JOHNSON J. D. Specific degradation of Cryptococcus neoformans 3723 capsular polysaccharide by a microbial enzyme. I. Isolation, partial purification, and properties of the enzyme. Can J Microbiol. 1961 Feb;7:53–60. doi: 10.1139/m61-007. [DOI] [PubMed] [Google Scholar]
  5. GADEBUSCH H. H. Specific degradation of Cryptococcus neoformans 3723 capsular polysaccharide by a microbial enzyme. II. Biological activity of the enzyme. J Infect Dis. 1960 Nov-Dec;107:402–405. doi: 10.1093/infdis/107.3.402. [DOI] [PubMed] [Google Scholar]
  6. GILMORE T. E., HOWE C. An aerobic soil microorganism which decomposes blood group substances. I. Metabolic and immunochemical studies. J Bacteriol. 1959 Dec;78:805–813. doi: 10.1128/jb.78.6.805-813.1959. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. HOWE C., MACLENNAN J. D., MANDL I., KABAT E. A. Enzymes of Clostridium tertium: effects on blood group and virus receptor substances. J Bacteriol. 1957 Sep;74(3):365–376. doi: 10.1128/jb.74.3.365-376.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. JARVIS F. G., MESENKO M. T., KYLE J. E. Electrophoretic purification of the Vi antigen. J Bacteriol. 1960 Nov;80:677–682. doi: 10.1128/jb.80.5.677-682.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. KRAUSE R. M., MCCARTY M. Studies on the chemical structure of the streptococcal cell wall. I. The identification of a mucopeptide in the cell walls of groups A and A-variant streptococci. J Exp Med. 1961 Jul 1;114:127–140. doi: 10.1084/jem.114.1.127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LANDY M., LAMB E. Estimation of Vi antibody employing erythrocytes treated with purified Vi antigen. Proc Soc Exp Biol Med. 1953 Apr;82(4):593–598. doi: 10.3181/00379727-82-20188. [DOI] [PubMed] [Google Scholar]
  11. MCCARTY M. The lysis of group A hemolytic streptococci by extracellular enzymes of Streptomyces albus. I. Production and fractionation of the lytic enzymes. J Exp Med. 1952 Dec;96(6):555–568. doi: 10.1084/jem.96.6.555. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. MCCARTY M. The lysis of group A hemolytic streptococci by extracellular enzymes of Streptomyces albus. II. Nature of the cellular substrate attacked by the lytic enzymes. J Exp Med. 1952 Dec;96(6):569–580. doi: 10.1084/jem.96.6.569. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. McCARTY M. Further studies on the chemical basis for serological specificity of Group A streptococcal carbohydrate. J Exp Med. 1958 Sep 1;108(3):311–323. doi: 10.1084/jem.108.3.311. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. McCARTY M., LANCEFIELD R. C. Variation in the group-specific carbohydrate of group A streptococci. I. Immunochemical studies on the carbohydrates of variant strains. J Exp Med. 1955 Jul 1;102(1):11–28. doi: 10.1084/jem.102.1.11. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Sickles G. M., Shaw M. A Systematic Study of Microörganisms Which Decompose the Specific Carbohydrates of the Pneumococcus. J Bacteriol. 1934 Oct;28(4):415–431. doi: 10.1128/jb.28.4.415-431.1934. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. TORRIANI A., PAPPENHEIMER A. M., Jr Inducible polysaccharide depolymerases of Bacillus palustris. J Biol Chem. 1962 Jan;237:3–13. [PubMed] [Google Scholar]
  17. WHITESIDE R. E., BAKER E. E. Antigenic analysis of Salmonella typhosa and related salmonellas. J Immunol. 1962 May;88:650–660. [PubMed] [Google Scholar]

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