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Cited by 165

The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.

Identification and molecular analysis of a locus that regulates extracellular toxin production in Clostridium perfringens

Lyristis, Michael, Bryant, Amy E., Sloan, Joan, Awad, Milena M., Nisbet, Ian T., Stevens, Dennis L., Rood, Julian I.·1994·Molecular Microbiology
DOI 10.1111/j.1365-2958.1994.tb01063.x
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Abstract

Summary: The anaerobic bacterium Clostridium perfringens mediates clostridial myonecrosis, or gas gangrene, by producing a number of extracellular toxins and enzymes. Transposon mutagenesis with Tn916 was used to isolate a pleiotropic mutant of C. perfringens that produced reduced levels of phospholipase C, protease and sialidase, and did not produce any detectable perfringolysin O activity. Southern hybridization revealed that a single copy of Tn 916 had inserted into a 2.7 kb Hin dlll fragment in the C. perfringens chromosome. A 4.3 kb Pstl fragment, which spanned the Tn 916 insertion site, was cloned from the wild‐type strain. When subcloned into a shuttle vector and introduced into C. perfringens this fragment was able to complement the Tn916‐derived mutation. Transformation of the mutant with plasmids containing the 2.7 kb Hin dlll fragment, or the 4.3 kb Pst l fragment resulted in toxin and enzyme levels greater than or equal to those of the wild‐type strain. The Pst l fragment was sequenced and found to potentially encode seven open reading frames, two of which appeared to be arranged in an operon and shared sequence similarity with members of two‐component signal transduction systems. The putative virR gene encoded a protein with a deduced molecular weight of 30140, and with sequence similarity to activators in the response regulator family of proteins. The next gene, virS, into which Tn 916 had inserted, was predicted to encode a membrane‐spanning protein with a deduced molecular weight of 51 274. The putative VirS protein had sequence similarity to sensor proteins and also contained a histidine residue highly conserved in the histidine protein kinase family of sensor proteins. Virulence studies carried out using a mouse model implicated the virS gene in the pathogenesis of histotoxic C. perfringens infections. It was concluded that a two‐component sensor regulator system that activated the expression of a number of extracellular toxins and enzymes involved In virulence had been cloned and sequenced. A model that described the regulation of extracellular toxin production in C. perfringens was constructed.

Overview

Integrity signals

Registry

Crossref · 10.1111/j.1365-2958.1994.tb01063.x

Cites

75 of 75 references verified0 citation errors · 0 not checkable

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Citations

Cites

Research works printed but not linked: 10

  1. 10.1016/S0022-2836(05)80360-2 · DOI · Paper page
  2. Burdett V., 1982, Microbiology, 155
  3. 10.1111/j.1574-6968.1993.tb05873.x · DOI
  4. Higashi Y., 1973, Complementation of θ‐toxigenicity between mutants of two groups of Clostridium perfringens, Biken J, 16, 1
  5. Imagawa T., 1981, Complentation characteristics of newly isolated mutants from two groups of strains of Clostridium perfringens, Biken J, 24, 13
  6. Lyall A., 1986, Parallel Computing, 235
  7. Morelle G., 1989, A plasmid extraction procedure on a miniprep scale, Focus, 11, 7
  8. Murphy E., 1989, Mobile DNA, 269
  9. 10.1128/mr.55.4.621-648.1991 · DOI · Paper page
  10. Smith M., 1990, High efficiency bacterial electroporation: 1 × 1010 E. coli trans‐formants/mg, Focus, 12, 38

Cited by

See all 165

Metadata

Authors
Lyristis, M., Bryant, A. E., Sloan, J., Awad, M. M., Nisbet, I. T., Stevens, D. L., & Rood, J. I.
Venue
Molecular Microbiology
Publisher
Wiley
Published
1994-06
Volume
12
Issue
5
Pages
761-777
ISSN
  • 0950-382X
  • 1365-2958
DOI
10.1111/j.1365-2958.1994.tb01063.x
Cited by
165
References
75
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 4531 d)

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Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.