1887

Abstract

Summary

Chancroid is a sexually transmitted diseased caused by A. The pathological manifestations of chancroid are unique among species and the virulence factors of that account for these features have not been identified. Some of these virulence factors may be unique components of , but attempts to identify -specific components have been unsuccessful. Four polypeptides—A, B, C and D of 83, 77, 56 and 28 kDa, respectively—were identified with a panel of nine -specific monoclonal antibodies (MAbs). Polypeptide C was one of the five major proteins in and demonstrated micro-heterogeneity in SDS-PAGE. Polypeptides A, B and D were present in only small amounts in whole-cell lysates of The relative amounts of A and B varied, suggesting that they may be precursor molecules. The unique polypeptides C and D were not exposed on the surface. Polypeptide C was highly soluble and did not appear to be membrane-bound, whereas polypeptide D appeared to partition with the cytoplasmic membrane and was soluble in Sarkosyl. All four polypeptides appeared to be unique to since MAbs directed against them did not cross-react with or The mol. wts of all of these polypeptides were conserved throughout 35 clinical isolates collected from 15 cities in eight countries and one reference strain of that were tested. Based on the immune cross-reactivities, it was concluded that the four polypeptides belonged to a family of proteins with partial sequence homology that may have been derived from the same precursor polypeptide or the same transcription unit. A sequence relationship model for the polypeptides was proposed based on their cross-reactivities with the MAbs.

Loading

Article metrics loading...

/content/journal/jmm/10.1099/00222615-37-6-413
1992-12-01
2024-12-01
Loading full text...

Full text loading...

/deliver/fulltext/jmm/37/6/medmicro-37-6-413.html?itemId=/content/journal/jmm/10.1099/00222615-37-6-413&mimeType=html&fmt=ahah

References

  1. Johnson A. P., Abeck D., Davies H. A. The structure, pathogenicity and genetics of Haemophilus ducreyi. J Infect 1988; 17:99–106
    [Google Scholar]
  2. Morse S. A. Chancroid and Haemophilus ducreyi. Clin Microbiol Rev 1989; 2:137–157
    [Google Scholar]
  3. Slootmans L., Vanden Berghe D. A., Piot P. Typing Haemophilus ducreyi by indirect immunofluorescence assay. Genitourin Med 1985; 61:123–126
    [Google Scholar]
  4. Saunders J. M., Folds J. D. Immunoblot analysis of antigens associated with Haemophilus ducreyi using serum from immunised rabbits. Genitourin Med 1986; 62:321–328
    [Google Scholar]
  5. Museyi K., Van Dyck E., Vervoort T., Taylor D., Hoge C., Piot P. Use of an enzyme immunoassay to detect serum IgG antibodies to Haemophilus ducreyi. J Infect Dis 1988; 157:1039–1043
    [Google Scholar]
  6. Odumeru J. A., Alfa M. J., Martin C. F., Ronald A. R., Jay F. T. Production of monoclonal antibodies specific for Haemophilus ducreyi: a screening method to discriminate specific and cross-reacting antibodies. Hybridoma 1989; 8:337–351
    [Google Scholar]
  7. Hansen E. J., Loftus T. A. Monoclonal antibodies reactive with all strains of Haemophilus ducreyi. Infect Immun 1984; 44:196–198
    [Google Scholar]
  8. Schalla W. O., Sanders L. L., Schmid G. P., Tam M. R., Morse S. A. Use of dot-immunobinding and immunofluorescence assays to investigate clinically suspected cases of chancroid. J Infect Dis 1986; 153:879–887
    [Google Scholar]
  9. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–685
    [Google Scholar]
  10. Fraker P. J., Speck J. C. Protein and cell membrane iodinations with a sparingly soluble chloroamide 1, 3, 4, 6-tetrachloro-3a, 6a-diphenylglycoluril. Biochem Biophys Res Commun 1978; 80:849–857
    [Google Scholar]
  11. Abeck D., Johnson A. P., Taylor-Robinson D. Antigenic analysis of Haemophilus ducreyi by Western blotting. Epidemiol Infect 1988; 101:151–157
    [Google Scholar]
  12. Abeck D., Johnson A. P. Identification of surface-exposed proteins Haemophilus ducreyi. FEMS Microbiol Lett 1987; 44:49–51
    [Google Scholar]
  13. Odumeru J. A., Ronald A. R., Albritton W. L. Characterization of cell proteins of Haemophilus ducreyi by polyacrylamide gel electrophoreses. J Infect Dis 1983; 148:710–714
    [Google Scholar]
  14. Carlone G. M., Thomas M. L., Rumschlag H. S., Sottnek F. O. Rapid microprocedure for isolating detergent-insoluble outer membrane proteins from Haemophilus species. J Clin Microbiol 1986; 24:330–332
    [Google Scholar]
  15. Barenkamp S. J., Munson R. S., Granoff D. M. Subtyping isolates of Haemophilus influenzae type b by outer membrane protein profiles. J Infect Dis 1981; 143:668–676
    [Google Scholar]
  16. Tewari R. P., Lynn M., Bimbaum A. J., Solotorovsky M. Characterization of the immunoprotective antigen of ribosomal preparations of Haemophilus influenzae. Infect Immun 1978; 19:58–65
    [Google Scholar]
  17. Cabrera-Contreras R., Plescia O., Solotorovsky M., Lynn M. Enhancement of immunogenic activity of ribosomal preparations from Haemophilus influenzae by various adjuvants. Vaccine 1985; 3:103–108
    [Google Scholar]
  18. Simonsen J. N., Cameron D. W., Gakinya M. N. Human immune-deficiency virus infection among men with sexually transmitted diseases. Experience from a centre in Africa. N Engl J Med 1988; 319:274–278
    [Google Scholar]
  19. Pepin J., Plummer F. A., Brunham R. C., Piot P., Cameron D. W., Ronald A. R. The interaction of HIV infection and other sexually transmitted diseases: an opportunity for intervention. AIDS 1989; 3:3–9
    [Google Scholar]
/content/journal/jmm/10.1099/00222615-37-6-413
Loading
/content/journal/jmm/10.1099/00222615-37-6-413
Loading

Data & Media loading...

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