• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of jbacterPermissionsJournals.ASM.orgJournalJB ArticleJournal InfoAuthorsReviewers
J Bacteriol. Apr 1987; 169(4): 1509–1515.
PMCID: PMC211976

The secreted hemolysins of Proteus mirabilis, Proteus vulgaris, and Morganella morganii are genetically related to each other and to the alpha-hemolysin of Escherichia coli.


Secreted hemolysins were extremely common among clinical isolates of Proteus mirabilis, Proteus vulgaris, and Morganella morganii, and hemolytic activity was either cell associated or cell free. Southern hybridization of total DNA from hemolytic isolates to cloned regions of the Escherichia coli alpha-hemolysin (hly) determinant showed clear but incomplete homology between genes encoding production of hemolysins in the four species. One of the two E. coli secretion genes, hlyD, hybridized only with DNA from P. vulgaris and M. morganii, which produced cell-free hemolysis, but not with that from P. mirabilis, which showed only cell-associated activity. Molecular cloning of the genetic determinants of cell-free hemolytic activity from P. vulgaris and M. morganii chromosomal DNA allowed their functional analysis via inactivation with the transposons Tn1000 and Tn5. Both hemolysin determinants were about 7.5 kilobase pairs and comprised contiguous regions directing regulation, synthesis, and specific secretion out of the cell. Transposon mutations which eliminated secretion of the Proteus and Morganella hemolysins could be complemented specifically by the E. coli hemolysin secretion genes hlyB or hlyD. Alignment of the physically and functionally defined hly determinants from P. vulgaris and M. morganii with that of the E. coli alpha-hemolysin confirmed a close genetic relationship but also indicated extensive evolutionary divergence.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.4M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Berg DE, Davies J, Allet B, Rochaix JD. Transposition of R factor genes to bacteriophage lambda. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3628–3632. [PMC free article] [PubMed]
  • Cavalieri SJ, Bohach GA, Snyder IS. Escherichia coli alpha-hemolysin: characteristics and probable role in pathogenicity. Microbiol Rev. 1984 Dec;48(4):326–343. [PMC free article] [PubMed]
  • Debouck C, Riccio A, Schumperli D, McKenney K, Jeffers J, Hughes C, Rosenberg M, Heusterspreute M, Brunel F, Davison J. Structure of the galactokinase gene of Escherichia coli, the last (?) gene of the gal operon. Nucleic Acids Res. 1985 Mar 25;13(6):1841–1853. [PMC free article] [PubMed]
  • de la Cruz F, Zabala JC, Ortiz JM. Hemolysis determinant common to Escherichia coli strains of different O serotypes and origins. Infect Immun. 1983 Sep;41(3):881–887. [PMC free article] [PubMed]
  • Felmlee T, Pellett S, Lee EY, Welch RA. Escherichia coli hemolysin is released extracellularly without cleavage of a signal peptide. J Bacteriol. 1985 Jul;163(1):88–93. [PMC free article] [PubMed]
  • Felmlee T, Pellett S, Welch RA. Nucleotide sequence of an Escherichia coli chromosomal hemolysin. J Bacteriol. 1985 Jul;163(1):94–105. [PMC free article] [PubMed]
  • Fry DC, Kuby SA, Mildvan AS. ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins. Proc Natl Acad Sci U S A. 1986 Feb;83(4):907–911. [PMC free article] [PubMed]
  • Gerlach JH, Endicott JA, Juranka PF, Henderson G, Sarangi F, Deuchars KL, Ling V. Homology between P-glycoprotein and a bacterial haemolysin transport protein suggests a model for multidrug resistance. Nature. 1986 Dec 4;324(6096):485–489. [PubMed]
  • Gray L, Mackman N, Nicaud JM, Holland IB. The carboxy-terminal region of haemolysin 2001 is required for secretion of the toxin from Escherichia coli. Mol Gen Genet. 1986 Oct;205(1):127–133. [PubMed]
  • Gros P, Croop J, Housman D. Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins. Cell. 1986 Nov 7;47(3):371–380. [PubMed]
  • Guyer MS. Uses of the transposon gamma delta in the analysis of cloned genes. Methods Enzymol. 1983;101:362–369. [PubMed]
  • Hacker J, Hughes C. Genetics of Escherichia coli hemolysin. Curr Top Microbiol Immunol. 1985;118:139–162. [PubMed]
  • Higgins CF, Hiles ID, Salmond GP, Gill DR, Downie JA, Evans IJ, Holland IB, Gray L, Buckel SD, Bell AW, et al. A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria. Nature. 1986 Oct 2;323(6087):448–450. [PubMed]
  • Jakes KS, Model P. Mechanism of export of colicin E1 and colicin E3. J Bacteriol. 1979 Jun;138(3):770–778. [PMC free article] [PubMed]
  • Jorgensen RA, Rothstein SJ, Reznikoff WS. A restriction enzyme cleavage map of Tn5 and location of a region encoding neomycin resistance. Mol Gen Genet. 1979;177(1):65–72. [PubMed]
  • Juarez A, Hughes C, Vogel M, Goebel W. Expression and regulation of the plasmid-encoded hemolysin determinant of Escherichia coli. Mol Gen Genet. 1984;197(2):196–203. [PubMed]
  • Knapp S, Hacker J, Then I, Müller D, Goebel W. Multiple copies of hemolysin genes and associated sequences in the chromosomes of uropathogenic Escherichia coli strains. J Bacteriol. 1984 Sep;159(3):1027–1033. [PMC free article] [PubMed]
  • Mackman N, Holland IB. Functional characterization of a cloned haemolysin determinant from E. coli of human origin, encoding information for the secretion of a 107K polypeptide. Mol Gen Genet. 1984;196(1):129–134. [PubMed]
  • Mackman N, Nicaud JM, Gray L, Holland IB. Genetical and functional organisation of the Escherichia coli haemolysin determinant 2001. Mol Gen Genet. 1985;201(2):282–288. [PubMed]
  • Mackman N, Nicaud JM, Gray L, Holland IB. Secretion of haemolysin by Escherichia coli. Curr Top Microbiol Immunol. 1986;125:159–181. [PubMed]
  • Müller D, Hughes C, Goebel W. Relationship between plasmid and chromosomal hemolysin determinants of Escherichia coli. J Bacteriol. 1983 Feb;153(2):846–851. [PMC free article] [PubMed]
  • Palva ET, Hirst TR, Hardy SJ, Holmgren J, Randall L. Synthesis of a precursor to the B subunit of heat-labile enterotoxin in Escherichia coli. J Bacteriol. 1981 Apr;146(1):325–330. [PMC free article] [PubMed]
  • Senior BW. Typing of Proteus strains by proticine production and sensitivity. J Med Microbiol. 1977 Feb;10(1):7–17. [PubMed]
  • So M, McCarthy BJ. Nucleotide sequence of the bacterial transposon Tn1681 encoding a heat-stable (ST) toxin and its identification in enterotoxigenic Escherichia coli strains. Proc Natl Acad Sci U S A. 1980 Jul;77(7):4011–4015. [PMC free article] [PubMed]
  • Stark JM, Shuster CW. The structure of cloned hemolysin DNA from plasmid pHly185. Plasmid. 1983 Jul;10(1):45–54. [PubMed]
  • Wagner W, Vogel M, Goebel W. Transport of hemolysin across the outer membrane of Escherichia coli requires two functions. J Bacteriol. 1983 Apr;154(1):200–210. [PMC free article] [PubMed]
  • Welch RA, Hull R, Falkow S. Molecular cloning and physical characterization of a chromosomal hemolysin from Escherichia coli. Infect Immun. 1983 Oct;42(1):178–186. [PMC free article] [PubMed]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)


Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...


Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...