1887

Abstract

The biochemical, immunological, and biological properties of an S layer purified from an strain (AH-342) involved in a case of bacteraemia were investigated. The S layer selectively removed from the cell surface was composed of a single acidic (pI 4·65) protein subunit (surface array protein, SAP) with a molecular mass of approximately 52 kDa. Amino acid analysis of this 52 kDa protein indicated a molecule composed of 498 amino acids with 46% hydrophobic residues. No cysteine residues were detected. The first 35 residues of the N-terminus were sequenced by Edman degradation; only 4–24% homology was noted between this sequence and those previously published for SAPs of (A450) and a strain of (TF7) originally isolated from a moribund fish. Polyclonal antibodies raised against AH-342 SAP were genospecific, reacting only against S layers produced by strains and not those from . Acute serum from the bacteraemic patient from whom AH-342 was isolated reacted strongly with the SAP of AH-342 in immunoblot studies. Purified SAP, when intraperitoneally co-inoculated with SAP strains of into Swiss-Webster mice, could reduce the 50% lethal dose by approximately 30–70 fold. The results suggest that the SAP of strains may play an important role in systemic dissemination after invasion through the gastrointestinal mucosa.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-138-6-1229
1992-06-01
2022-01-17
Loading full text...

Full text loading...

/deliver/fulltext/micro/138/6/mic-138-6-1229.html?itemId=/content/journal/micro/10.1099/00221287-138-6-1229&mimeType=html&fmt=ahah

References

  1. Dooley J. S. G, McCubbin W. D., Kay C. M., Trust T. J. 1988 a; Isolation and biochemical characterization of the S layer protein from a pathogenic Aeromonas hydrophila strain. Journal of Bacteriology 170:2631–2638
    [Google Scholar]
  2. Dooley J. S. G, Trust T. J. 1988b; Surface protein composition of Aeromonas hydrophila strains virulent for fish : identification of a surface array protein. Journal of Bacteriology 170:499–506
    [Google Scholar]
  3. Falkow S. 1990; The ‘Zen’ of bacterial pathogenicity. Molecular Basis of Bacterial Pathogenesis. Iglewski B. H., Clark V. L. Academic Press: San Diego;
    [Google Scholar]
  4. Gill D. M. 1982; Bacterial toxins: a table of lethal amounts. Microbiological Reviews 46:86–94
    [Google Scholar]
  5. Griffiths S. G., Lynch W. H. 1990; Characterization of Aeromonas salmonicida variants with altered cell surfaces and their use in studying surface protein assembly. Archives of Microbiology 154:308–312
    [Google Scholar]
  6. Ho A. S. Y, Mietnzer Τ. Α., Smith A. J., Schoolnik G. K. 1990; The pili of Aeromonas hydrophila: identification of an environmentally regulated ‘mini pilin.’. Journal of Experimental Medicine 172:795–806
    [Google Scholar]
  7. Janda J. M. 1991; Recent advances on the taxonomy, pathogenicity, and infectious syndromes associated with the genus Aeromonas . Clinical Microbiology Reviews 4:397–410
    [Google Scholar]
  8. Janda J. M., Oshiro L. S., Abbott S. L., Duffey P. S. 1987; Virulence markers of mesophilic aeromonads: association of the autoagglutination phenomenon with mouse pathogenicity and the presence of a peripheral cell-associated layer. Infection and Immunity 55:3070–3077
    [Google Scholar]
  9. Kokka R. P., Janda J. M. 1990; Isolation and identification of autoagglutinating serogroup 0:11 Aeromonas strains in the clinical laboratory. Journal of Clinical Microbiology 28:1297–1299
    [Google Scholar]
  10. Kokka R. P., Vedros N. A., Janda J. M. 1990; Electrophoretic analysis of the surface components of autoagglutinating surface array protein-positive and surface array protein-negative Aeromonas hydrophila and Aeromonas sobria . Journal of Clinical Microbiology 28:2240–2247
    [Google Scholar]
  11. Kokka R. P., Janda J. M., Oshiro L. S., Altwegg M., Shimada T., Sakazaki R., Brenner D. J. 1991a; Biochemical and genetic characterization of autoagglutinating phenotypes of Aeromonas species associated with invasive and noninvasive disease. Journal of Infectious Diseases 163:890–894
    [Google Scholar]
  12. Kokka R. P., Vedros N. A., Janda J. M. 1991b; Characterization of classic and atypical serogroup 0:11 Aeromonas: evidence that the surface array protein is not directly involved in mouse pathogenicity. Microbial Pathogenesis 10:71–79
    [Google Scholar]
  13. Koval S. F., Hynes S. H. 1991; Effect of paracrystalline protein surface layers on prédation by Bdellovibrio bacteriovorus . Journal of Bacteriology 173:2244–2249
    [Google Scholar]
  14. Paula S. J., Duffey P. S., Abbott S. L., Kokka R. P., Oshiro L. S., Janda J. M., Shimada T., Sakazaki R. 1988; Surface properties of autoagglutinating mesophilic aeromonads. Infection and Immunity 56:2658–2665
    [Google Scholar]
  15. Sleytr U. B., Messner P. 1983; Crystalline surface layers on bacteria. Annual Reviews of Microbiology 37:311–339
    [Google Scholar]
  16. Sleytr U. B., Messner P. 1988; Crystalline surface layers on procaryotes. Journal of Bacteriology 170:2891–2897
    [Google Scholar]
  17. Trust T. J. 1986; Pathogenesis of infectious diseases offish. Annual Review of Microbiology 40:479–502
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-138-6-1229
Loading
/content/journal/micro/10.1099/00221287-138-6-1229
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error