Molecular and General Genetics MGG

, Volume 200, Issue 3, pp 472–475 | Cite as

Cellular localization and export of the soluble haemolysin of Vibrio cholerae El Tor

  • Antonietta Mercurio
  • Paul A. Manning


The cellular location of the haemolysin of Vibrio cholerae El Tor strain 017 has been analyzed. This protein is found both in the periplasmic space and the extracellular medium in Vibrio cholerae. However, when the cloned gene, present on plasmid pPM431, is introduced into E. coli K-12 this protein remains localized predominantly in the periplasmic space with no activity detected in the extracellular medium. Mutants of E. coli K-12 (tolA and tolB) which leak periplasmic proteins mimic excretion and release the haemolysin into the growth medium. Secretion of haemolysin into the periplasm is independent of perA (envZ) and in fact, mutants in perA (envZ) harbouring pPM431 show hyperproduction of periplasmic haemolysin. These results in conjunction with those for other V. cholerae extracellular proteins suggest that although E. coli K-12 can secrete these proteins into the periplasm, it lacks a specific excretion mechanism, present in V. cholerae, for the release of soluble proteins into the growth medium.


Growth Medium Soluble Protein Vibrio Cellular Localization Extracellular Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Achtman M, Schwuchow S, Helmuth R, Morelli G, Manning PA (1978) Cell-cell interactions in conjugating Escherichia coli; Con- mutants and stabilization of mating aggregates. Mol Gen Genet 164:171–183Google Scholar
  2. Anderson JJ, Wilson JM, Oxender DL (1979) Defective transport and other phenotypes of a periplasmic ‘leaky’ mutant of Escherichia coli K-12. J Bacteriol 140:351–358Google Scholar
  3. Bernstein A, Rolfe B, Onodera K (1972) Pleiotropic effects and genetic organization of the tolAB locus of Escherichia coli K-12. J Bacteriol 112:74–83Google Scholar
  4. Brown HCM, Weston A, Saunders JR, Humphreys GO (1979) Transformation of E. coli C600 by plamsid DNA at different phases of growth. FEMS Microbiol Lett 5:219–222Google Scholar
  5. Ghrayeb J, Kimura H, Takahara M, Hsinng H, Masui Y, Inouye M (1984) Secretion cloning vectors in Escherichia coli. EMBO J 3:2437–2442Google Scholar
  6. Goebel W, Hedgpeth J (1982) Cloning and functional characterization of the plasmid-encoded haemolysin determinant of Escherichia coli. J Bacteriol 151:1290–1298Google Scholar
  7. Honda T, Finkelstein RA (1979) Purification and characterization of a hemolysin produced by Vibrio cholerae biotype El Tor; another toxic substance produced by cholera vibrios. Infect Immunol 20:1020–1027Google Scholar
  8. Lugtenberg B, Meijers J, Peters R, Van der Hoek P, Van Alphen L (1975) Electrophoretic resolution of the ‘major outer membrane protein’ of Escherichia coli K-12 into four bands. FEBS Lett 58:254–258Google Scholar
  9. Manning PA, Brown MH, Heuzenroeder MW (1984) Cloning of the structural gene (hly) for the haemolysin of Vibrio cholerae El Tor strain 017. Gene 31:225–231Google Scholar
  10. Michaelis S, Beckwith J (1982) Mechanism of incorporation of cell envelope proteins in Escherichia coli. Annu Rev Microbiol 36:435–465Google Scholar
  11. Morona R, Reeves P (1981) Molecular cloning of the tolC locus of Escherichia coli K-12 with the use of the transposon Tn10. Mol Gen Genet 184:430–433Google Scholar
  12. Morona R, Reeves P (1982) The tolC locus of Escherichia coli K-12 affects the expression of three major outer membrane proteins. J Bacteriol 150:1016–1023Google Scholar
  13. Osborn MJ, Gander JE, Parisi E, Carson J (1972) Mechanism of assembly of the outer membrane of Salmonella typhimurium. J Biol Chem 247:3962–3972Google Scholar
  14. Pearson GDN, Mekalanos JJ (1982) Molecular cloning of Vibrio cholerae enterotoxin genes in Escherichia coli K-12. Proc Natl Acad Sci USA 79:2976–2980Google Scholar
  15. Pollitzer R (1959) Cholera. Monograph series, No. 43. World Health Organisation, GenevaGoogle Scholar
  16. Wanner BL, Sarthy A, Beckwith J (1979) Escherichia coli pleiotropic mutant that reduced amounts of several periplasmic and outer membrane proteins. J Bacteriol 140:229–239Google Scholar
  17. Yamamoto K, Alo-omani M, Honda T, Takeda Y, Miwatani T (1984) Non-Ol Vibrio cholerae hemolysin: purification, partial characterization, and immunological relatedness to El Tor hemolysin. Infect Immunol 45:192–196Google Scholar

Copyright information

© Springer-Verlag 1985

Authors and Affiliations

  • Antonietta Mercurio
    • 1
  • Paul A. Manning
    • 1
  1. 1.Department of Microbiology and ImmunologyThe University of AdelaideAdelaideAustralia

Personalised recommendations