Pleiotropic consequences of mutations towards antibiotic-hypersensitivity in Serratia marcescens

Winkler, U.; Heller, Klaus B.; Folle, B

doi:10.1007/bf00417849

Cited by 23 publications

(19 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…From our results and other worker's studies (1,3,6), it was suggested that the hypersensitivity to p-lactam antibiotics of hypersensitive mutants is associated with not only the loss of p-lactamase productivity, but also the increased susceptibility to lysis by detergents such as SDS (7) or sarkosy (1) which attack the outer membrane. …”

supporting

confidence: 68%

“…1, B and C). The increased susceptibility to lysis by detergents such as SDS has been considered to be due to outer membrane mutation in the mutants from E. coli (1), P. aeruginosa (3), and S. marcescens (6). There- fore, triton-, sarkosyl-, and SDS-insoluble membrane fractions of the strain Pre and the parents strain were prepared by treatment with concentrations of 2°1, of each detergent for 30 min at 25 C as described by Whitfield et al (5), and applied to a continuous system of SDS-polyacrylamide gel electrophoresis (SDS-PAGE) (2) using 12(() acrylamide (Fig.…”

mentioning

confidence: 99%

See 1 more Smart Citation

The Pleiotropic Properties of a Beta‐Lactam Antibiotic‐Hypersensitive Mutant Derived from Proteus vulgaris IFO 3167

Hamakado

Yoshida

Kido

et al. 1985

Microbiology and Immunology

View full text Add to dashboard Cite

supporting

confidence: 68%

mentioning

confidence: 99%

The Pleiotropic Properties of a Beta‐Lactam Antibiotic‐Hypersensitive Mutant Derived from Proteus vulgaris IFO 3167

Hamakado

Yoshida

Kido

et al. 1985

Microbiology and Immunology

View full text Add to dashboard Cite

“…A few nonpigmented colonies which produced protease were found, but these were rare. The correlation between pigmentation and protease production has been observed by others (40). The rleationship between the unstable pigmentation phenotype and expression of the protease is not clear.…”

Section: Resultsmentioning

confidence: 83%

Genetic analysis of extracellular proteins of Serratia marcescens

et al. 1988

View full text Add to dashboard Cite

Serratia marcescens, a gram-negative enteric bacterium, is capable of secreting a number of proteins extraceliularly. The types of activity found in the growth media include proteases, chitinases, a nuclease, and a lipase. Genetic studies have been undertaken to investigate the mechanisms used for the extracellular secretion of these exoproteins by S. marcescens. Many independent mutations affecting the extracellular enzymes were isolated after chemical and transposon mutagenesis. Using indicator media, we have identified loci involved in the production or excretion of extraceliular protease, nuclease, or chitinase by S. marcescens. None of the mutations represented general extracellular-excretion mutants; in no case was the production or excretion of multiple exoproteins affected. A variety of loci were identified, including regulatory mutations affecting nuclease and chitinase expression. A number of phenotypically different protease mutants arose. Some of them may represent different gene products required for the production and excretion of the major metalioprotease, a process more complex than that for the other S. marcescens exoproteins characterized to date.The movement of molecules from the site of synthesis to a new location is a fundamental property of biological systems. Protein export to the cell envelope has been the object of intensive study in Escherichia coli (4), and mutations affecting this process have been identified (18,30). Many of these mutations are conditional, demonstrating that protein export to the cell envelope is essential to the cell. The extracellular secretion (or excretion) of some proteins into the growth medium can also be achieved by some bacteria (29, 32), although enteric bacteria as a group are not renowned for their ability to excrete proteins. In fact, E. coli only excretes proteins when it carries extrachromosomal elements specifying exoproteins. For some proteins, such as a-hemolysin, bacteriocins, and toxins (14,19,22,26,32), the release of the exoprotein usually requires the presence of other gene products; this implies that E. coli is not normally endowed with a general extracellular secretory system. Since E. coli is such a limited system for studying extracellular proteins, a range of other organisms has been investigated (29,32). Usually the exoproteins these organisms excrete are either toxins or degradatory proteins like proteases and nucleases.Some steps, such as signal sequence (31) recognition and processing, may be common to both envelope and extracellular protein translocation. Genes required for the export of both membrane-bound and extracellular proteins are essential to the cell, but genes required only for excretion appear not to be essential. By isolating mutants that are defective only in the excretion of extracellular proteins, it may be possible to separate this mechanism from envelope secretion.Mutations in Pseudomonas aeruginosa strains defective in the excretion of certain extracellular proteins have been isolated (41) formation of many but not ...

show abstract

“…Lipase activity (39) and synthesis of the pigment prodigiosin (unpublished observation) also decrease in rough strains of S. marcescens. Furthermore, a decrease in exocellular nuclease (16) and prodigiosin (38) production by S. marcescens has been correlated with an increase in the growth temperature from 30 to 37°C, parallel with alterations in LPS structure (this study).…”

Section: Methodsmentioning

confidence: 86%

Influence of growth temperature and lipopolysaccharide on hemolytic activity of Serratia marcescens

Poole

Braun

1988

J Bacteriol

View full text Add to dashboard Cite

Log-phase cells of Serrata marcescens cultured at 30°C were approximately 10-fold more hemolytic than those grown at 37°C. By using a cloned gene fusion of the promoter-proximal part of the hemolysin gene (shUi) to the Escherichia coli alkaline phosphatase gene (phoA), hemolysin gene expression as a function of alkaline phosphatase activity was measured at 30 and 370C. No difference in alkaline phosphatase activity was observed as a function of growth temperature, although more hemolysin was detectable immunologically in whole-cell extracts of cells grown at 300C. The influence of temperature was, however, growth phase dependent, because the hemolytic activities of cells cultured to early log phase at 30 and 37C were comparable. Given the outer membrane location of the hemolysin, lipopolysaccharide (LPS) was examined as a candidate for mediating the temperature effect on hemolytic activity. Silver staining of LPS in polyacrylamide gels revealed a shift towards shorter 0-antigen molecules at 370C relative to 300C. Moreover, there was less bimding of 0-antigen-specific bacteriophage to S. marcescens with increasing growth temperature, a finding consistent with temperaturemediated changes in LPS structure. Smooth strains of S. marcescens were 20-to 30-fold more hemolytic than rough derivatives, a result confirming that changes in LPS structure can influence hemolytic activity. The alkaline phosphatase activity of rough strains harboring the shl-phoA fusion was threefold lower than that of smooth strains harboring the fusion plasmids, a result consistent with a decrease in hemolysin gene expression in rough strains. The absence of a similar effect of temperature on gene expression may be related to less-marked changes in LPS structure as a function of temperature compared with a smooth-to-rough mutational change.

show abstract

Pleiotropic consequences of mutations towards antibiotic-hypersensitivity in Serratia marcescens

Cited by 23 publications

References 29 publications

The Pleiotropic Properties of a Beta‐Lactam Antibiotic‐Hypersensitive Mutant Derived from Proteus vulgaris IFO 3167

The Pleiotropic Properties of a Beta‐Lactam Antibiotic‐Hypersensitive Mutant Derived from Proteus vulgaris IFO 3167

Genetic analysis of extracellular proteins of Serratia marcescens

Influence of growth temperature and lipopolysaccharide on hemolytic activity of Serratia marcescens

Contact Info

Product

Resources

About