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PubMed1995

Extended-spectrum beta-lactamases conferring resistance to monobactams and oxyimino-cephalosporins in clinical isolates of Serratia marcescens.

We studied antibiotic resistance patterns and extended-spectrum beta-lactamases (ES beta Ls) production in Serratia marcescens strains isolated in our hospital during 1993. We examined 210 S. marcescens isolates. Of these, 172 were obtained from 49 patients admitted to an intensive care ward; 157 out of 172 were obtained from February to October and presented the same pattern of antibiotic resistance, including monobactams and oxyimino-cephalosporins. The remaining 15 out of 172 isolates (obtained from September to December) were susceptible to all drugs tested, with the exception of first generation cephalosporins. Thirty-eight additional isolates were recovered, during the same period, from 28 patients admitted to wards other than the intensive care unit; also these strains showed the high susceptibility pattern reported above. Epidemic strains of S. marcescens produced three different types of beta-lactamase with pI 5.4, 5.5, and 8.4. In contrast, non-epidemic strains produced only one type of beta-lactamase with pI 8.4. Conjugation experiments showed that the beta-lactamases having a pI of 5.4 and 5.5 (but not the one with pI 8.4) were plasmid-mediated. Since the beta-lactamase with pI 5.5 was capable of hydrolyzing monobactams and oxyimino-cephalosporins it was classified as ES beta L. Electrophoretic analysis showed that plasmids obtained from multiresistant strains were of about 54 kb; these plasmids appeared also to code for aminoglycoside resistance. Our data indicate that the plasmid-mediated production of ES beta Ls may contribute to the epidemic spread of Serratia marcescens in high-risk wards.

Aztreonam↗
PubMed2004

Serratia marcescens internalization and replication in human bladder epithelial cells.

BACKGROUND: Serratia marcescens, a frequent agent of catheterization-associated bacteriuria, strongly adheres to human bladder epithelial cells in culture. The epithelium normally provides a barrier between lumal organisms and the interstitium; the tight adhesion of bacteria to the epithelial cells can lead to internalization and subsequent lysis. However, internalisation was not shown yet for S. marcescens strains. METHODS: Elektronmicroscopy and the common gentamycin protection assay was used to assess intracellular bacteria. Via site directed mutagenesis, an hemolytic negative isogenic Serratia strain was generated to point out the importance of hemolysin production. RESULTS: We identified an important bacterial factor mediating the internalization of S. marcescens, and lysis of epithelial cells, as the secreted cytolysin ShlA. Microtubule filaments and actin filaments were shown to be involved in internalization. However, cytolysis of eukaryotic cells by ShlA was an interfering factor, and therefore hemolytic-negative mutants were used in subsequent experiments. Isogenic hemolysin-negative mutant strains were still adhesive, but were no longer cytotoxic, did not disrupt the cell culture monolayer, and were no longer internalized by HEp-2 and RT112 bladder epithelial cells under the conditions used for the wild-type strain. After wild-type S. marcescens became intracellular, the infected epithelial cells were lysed by extended vacuolation induced by ShlA. In late stages of vacuolation, highly motile S. marcescens cells were observed in the vacuoles. S. marcescens was also able to replicate in cultured HEp-2 cells, and replication was not dependent on hemolysin production. CONCLUSION: The results reported here showed that the pore-forming toxin ShlA triggers microtubule-dependent invasion and is the main factor inducing lysis of the epithelial cells to release the bacteria, and therefore plays a major role in the development of S. marcescens infections.

Anti-Bacterial Agents↗
PubMed2006

Purification and characterization of prodigiosin produced by integrated bioreactor from Serratia sp. KH-95.

To date, prodigiosin and its analogues which have been shown to have anticancer, cytotoxic and immunosuppressive activities have been isolated from Serratia, Pseudomonas and Streptomyces species, and chemically synthesized. In a previous study, the red pigment content in Serratia sp. KH-95 was enhanced using a casein-enriched medium. Recently, an integrated bioreactor with an internal adsorbent has been developed to increase the production yield and allow easy recovery of the pigment. Thus, this study focused on both purifying and identifying a single red pigment from several pigments attached to the adsorbent in an integrated bioreactor. The red pigment was extracted directly from the internal adsorbent using acidified methanol and phase separation. Subsequently, it was purified by silica gel chromatography and high performance liquid chromatograph (HPLC). As a result, pure prodigiosin was identified by structural studies as a pigment. Also, this downstream procedure that uses the integrated bioreactor can be applied to the direct production and purification of other prodigiosin analogues and hydrophobic alkaloid compounds from several microorganisms.

Bioreactors↗
PubMed1997

Isolation of propioxatin A from Actinosynnema sp. SI-23 during a screening for Serratia piscatorum metalloproteinase inhibitors.

An inhibitor of Serratia metalloproteinase was found in the cultured broth of strain SI-23, which was identified to be Actinosynnema sp. The inhibitor had a potent inhibitory effect on Serratia metalloproteinase and a weak effect on thermolysin, but no effect on other groups of proteinases. The structure of the inhibitor was deduced to be propioxatin A, reported as an enkephalinase B inhibitor.

Actinomycetales↗
PubMed1998

Chitin binding protein (CBP21) in the culture supernatant of Serratia marcescens 2170.

A chitin binding protein (CBP21) 21 kDa in size, is a major protein in the culture supernatant when Serratia marcescens 2170 is grown in the presence of chitin. The gene (cbp) for CBP21 was found to be located in a region 1.5 kb downstream of the chiB gene encoding chitinase B. The cbp gene encodes a polypeptide of 197 amino acids with a calculated size of 21.6 kDa containing a putative signal sequence of 27 amino acids. Comparison of the amino acid sequence of the deduced polypeptide with that of other proteins showed that CBP21 is similar (45.3% amino acid identity) to CHB1 of Streptomyces olivaceoviridis. Purified CBP21 prepared from the periplasmic fraction of Escherichia coli carrying the cloned cbp gene showed its highest binding activity to squid chitin (beta-chitin) followed by colloidal chitin and regenerated chitin. Binding of CBP21 to regenerated chitin was affected by pH, in particular, low pH reduced binding activity markedly. The presence of similar chitin binding proteins in the distantly related microorganisms, Streptomyces and Serratia, suggests a wide distribution of this type of chitin binding protein in chitinolytic microorganisms.

Amino Acid Sequence↗
PubMed1998

Purification and partial characterization of purine nucleoside phosphorylase from Serratia marcescens.

Purine nucleoside phosphorylase (PNP) was purified to homogeneity. The molecular weight of the enzyme was 170,000. The enzyme consisted of six subunits, each with a molecular weight of 27,000. Serratia PNP had ten times the affinity for adenosine and deoxyadenosine than for inosine and deoxyinosine in a pattern characteristic of bacterial PNP. 1-Methylinosine and 1-methylguanosine, which have no affinity for mammalian PNP, bound Serratia PNP. In terms of Kcat/K(m), the substrate specificities were in the descending order of guanosine, inosine, and adenosine. When inosine or deoxyinosine was used as a variable substrate, a biphasic reciprocal plot with upward curvature was observed. The values of the Hill coefficient were 1.2 and 1.1 for inosine and deoxyinosine, respectively. Positive cooperativity seemed to be involved in the binding of inosine and deoxyinosine to the enzyme.

Catalysis↗
PubMed2000

Analysis of oxidation sensitivity of maleate cis-trans isomerase from Serratia marcescens.

The maleate cis-trans isomerase gene (maiA) from Serratia marcescens IFO3736 was cloned and sequenced. Serratia MaiA has 62.4% amino acid identity with Alcaligenes faecalis IFO13111 MaiA and 64.9% with Bacillus stearothermophilus MI-102 MaiA. All known ten amino acid sequences of MaiA had significant conserved regions containing cysteine residues, which were previously suggested to be involved in an active site of the enzyme. The maiA gene was expressed in Escherichia coli, and expressed products MaiA was purified and characterized. The purified enzyme of strain IFO3736 showed high activity at room temperature and high heat stability. It also showed higher activity in the presence of high concentration of aspartic acid than the enzyme of A. faecalis IFO13111, but it was also sensitive to chemical oxidation. By amino acid composition analysis, cysteine, methionine, and tyrosine residues were suggested to be oxidized to inactivate the enzyme by chemical oxidation. To investigate the mechanism of chemical oxidation of the enzyme, six methionine residues in the conserved regions of S. marcescens MaiA were replaced with cysteine residues by site-directed mutagenesis. The analysis of the constructed mutants suggested that the Met201 residue near the Cys198 residue is involved in the sensitivity of the enzyme to chemical oxidation.

Amino Acid Sequence↗
PubMed1979

Serratia marcescens in tracheotomy cultures.

Twenty-three consecutive tracheotomies were cultured after an apparent outbreak of Serratia marcescens was noted. Over a period of one year, six cases with positive cultures were found. The importance of these positive cultures in relation to the patient's clinical course is discussed. The treatment of Serratia marcescens septicemia is reviewed.

Adult↗
PubMed1993

Microbial metabolism of quinoline and related compounds. XVIII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1.

Serratia marcecens 2CC-1 utilizes quinaldic acid (quinoline 2-carboxylic acid) as sole source of carbon, nitrogen and energy. Growth of strain 2CC-1 on quinaldic acid as well as on nicotinic acid and hypoxanthine was inhibited completely by the molybdate antagonist tungstate, whereas growth on kynurenic acid and 6-hydroxynicotinic acid was not affected by tungstate. The synthesis of the molybdenum-containing hydroxylases quinaldic acid 4-oxidoreductase and nicotinic acid 6-oxidoreductase was found to be inducible. In addition, Serratia marcescens 2CC-1 produced a constitutively expressed xanthine oxidoreductase. Quinaldic acid 4-oxidoreductase was purified 1075-fold with a recovery of 5%. For catalytic activity, artificial electron acceptors were necessary. The 95-100-kDa enzyme was a heterodimer with subunit molecular masses of 75-80 kDa and 18-19 kDa. Quinaldic acid 4-oxidoreductase contained 2.3-3.7 g atom of iron and 0.5-0.6 g atom of molybdenum per mol of enzyme. The absorption spectrum exhibited maxima at 280 nm, 334 nm, 480 nm and a shoulder at 550 nm, with A280/A334 = 4.8, A280/A450 = 10.0, A280/A480 = 9.4, and A450/A550 = 1.6, suggesting the absence of a flavin cofactor. Acridine, quinacrine, ethylenediaminetetraacetate, 2,2'-dipyridyl, 1,10-phenanthroline and iodoacetate did not affect enzyme activity. p-Hydroxymercuribenzoate, m-arsenite, cyanide and methanol were effective inhibitors of quinaldic acid 4-oxidoreductase. Cyanide-inhibited enzyme was reactivated by treatment with S2-, indicating the presence of a pterin molybdenum cofactor with a monooxo-monosulfidotype molybdenum center. Quinaldic acid 4-oxidoreductase showed a very high substrate specificity, quinaldic acid being the only substrate found to be transformed significantly.

Amino Acid Sequence↗
PubMedDate not supplied

Umbelliprenin from Ferula persica roots inhibits the red pigment production in Serratia marcescens.

The chloroform extract of Ferula persica var. persica roots was found to inhibit red pigment production of Serratia marcescens. A bioguided fractionation study by preparative thin layer chromatography (PTLC) detected a fraction (Rf = 0.71, petroleum ether/EtOAc, 2:1 v/v), which was effective on depigmentation of Serratia marcescens. Using conventional spectroscopy methods, the active fraction was identified as umbelliprenin. Neither the chloroform extract nor the isolated umbelliprenin fraction showed any antibacterial activity against the test strain at a certain concentration. In contrast, they exhibited depigmentation zones on culture plates.

Anti-Bacterial Agents↗
PubMed1981

Bacteriocin (marcescin) typing of clinically isolated Serratia marcescens.

A study of bacteriocin (marcescin) typing was carried out by an agar cross streaking method (without any induction reagent) with 654 strains of Serratia marcescens recently isolated from clinical materials in Nagasaki University Hospital. In a complete checker board experiment with 80 strains on bacteriocin production and sensitivity, 43 strains (54%) were productive, 74 (93%) were sensitive and 4 (5%) were negative. Immunity was confirmed in all strains. Eight out of 80 strains of Serratia marcescens were selected as indicators in order to achieve the best differentiation of strains in bacteriocin typing, and 654 strains were classified into 30 types by bacteriocin production typing and into 49 types by bacteriocin sensitivity typing; the former showed more stable results than the latter in reproducibility. Bacteriocins produced by this method were considered to be high molecular, phage tail-like group A bacteriocins reported by Prinsloo (1966). Bacteriocin production typing was more useful for classification and subdivision of strains than serotyping (0-group).

Bacteriocins↗
PubMed1984

Serratia marcescens in a newborn unit--microbiological features.

During a 12 mth period in a newborn unit (NBU), Serratia marcescens was isolated from 3 fatal cases of meningitis, 5 cases of septicemia, 5 of pneumonia, 4 or urinary tract infection and 15 of conjunctivitis. At the peak of the outbreak a 95% incidence of rectal colonization with S. marcescens was observed in the NBU. Polyacrylamide gel electrophoresis of sodium dodecylsulphate disrupted Serratia (SDS-PAGE) established that all isolates were identical.

Bacteriophage Typing↗
PubMed1989

Serratia bacteremia: a review of 44 episodes.

This report reviews 44 episodes of serratia bacteremia over a 9-year period (1980-1988) in a community-teaching hospital in the USA. The median age of patients was 64 years and 34% of the patients were older than 70 years. Nosocomial acquisition of bacteremia occurred in 70% of episodes, and 11% of patients were admitted from nursing homes. Nine episodes (20%) were polymicrobial bacteremia. The major portals of entry were the lower respiratory tract (11 episodes) and the urinary tract (6 episodes). The overall mortality was 52%. Factors that adversely influenced the mortality rate were rapidly fatal and ultimately fatal underlying conditions (p less than 0.001), platelet counts less than or equal to 100 x 10(0)/l at the onset of bacteremia (p less than 0.01), and total serum bilirubin greater than 18 mumol/l at the onset of bacteremia (p less than 0.01). All serratia strains tested were susceptible to gentamicin, kanamycin, amikacin and ceftizoxime.

Aged↗
PubMed2003

Purification and partial characterization of psychrotrophic Serratia marcescens lipase.

Serratia marcescens isolated from raw milk was found to produce extracellular lipase. The growth of this organism could contribute to flavor defects in milk and dairy products. Serratia marcescens was streaked onto spirit blue agar medium, and lipolytic activity was detected after 6 h at 30 degrees C and after 12 h at 6 degrees C. The extracellular crude lipase was collected after inoculation of the organism into nutrient broth and then into skim milk. The crude lipase was purified to homogeneity by ion-exchange chromatography and gel filtration. The purified lipase had a final recovered activity of 45.42%. Its molecular mass was estimated by SDS-PAGE assay to be 52 kDa. The purified lipase was characterized; the optimum pH was likely between 8 and 9 and showed about 70% of its activity at pH 6.6. The enzyme was very stable at pH 8 and lost about 30% of its activity after holding for 24 h at 4 degrees C in buffer of pH 6.6. The optimum temperature was observed at 37 degrees C and exhibited high activity at 5 degrees C. The thermal inactivation of S. marcescens lipase was more obvious at 80 degrees C; it retained about 15% of its original activity at 80 degrees C and was completely inactivated after heating at 90 degrees C for 5 min. Under optimum conditions, activity of the enzyme was maximum after 6 min. The Michaelis-Menten constant was 1.35 mM on tributyrin. The enzyme was inhibited by a concentration more than 6.25mM. Purified lipase was not as heat-stable as other lipases from psychrotrophs, but it retained high activity at 5 degrees C. At pH 6.6, the pH of milk, purified lipase showed some activity and stability. Also, the organism demonstrated lipolytic activity at 6 degrees C after 12 h. Therefore, S. marcescens and its lipase were considered to cause flavor impairment during cold storage of milk and dairy products.

Animals↗
PubMed1978

[Species specific esterase profiles in the genus Serratia].

Esterases of 62 Serratia marcescens, S. liquefaciens, S. plymuthica and S. marinorubra strains were analysed by electrophoresis in polyacrylamide-agarose gel. The comparative distribution of bands showed that the four Serratia species were characterized by distinct electrophoretic patterns of their esterases.

Esterases↗
PubMed1975

Cornea-damaging proteases of Serratia marcescens.

Fractionation of the culture supernatant fluids of Serratia marcescens, strain BG, by ammonium sulfate precipitation, isoelectric focusing, ion-exchange chromatography, hydroxyapatite adsorption chromatography, and gel filtration failed to separate the rabbit cornea-damaging activity and the in vitro protease activity of the preparations. Two proteases having similar molecular weights (44,000), estimated by gel filtration, and isoelectric points of approximately 5.0 and 5.3 were obtained free of detectable amounts of other known extracellular serratia enzymes. Heating a mixture of the two proteases for 15 minutes at 60 degrees C. resulted in complete loss of protease and cornea-damaging activities. Production of protease and cornea-damaging activities was inhibited by ammonium sulfate. The results support the conclusion that extracellular proteases produced in vitro by S. marcescens can elicit rapid and extensive damage to the rabbit cornea.

Ammonium Sulfate↗
PubMed2002

[Serratia marcescens vaccine in the treatment of malignant pleural effusion].

OBJECTIVE: To evaluate the efficacy and toxicity of Serratia marcescens (S311) vaccine in the treatment of malignant pleural effusion. METHODS: Thirty-four patients with malignant pleural effusion were given S311 as intrapleural injection with a dose of 10(9) U (0.32 mg) on D 1, 8 and 15, and observed for four weeks. RESULTS: The overall response rate (CR + PR) was 97.1% (CR in 12 patients and PR in 21 patients). The systemic toxicity was mild, including fever (82.4%), pleuritic pain (50.7%), nansea (26.5%), dyspnea (17.5%) and chills (5.9%). CONCLUSION: Serratia marcescens vaccine is effective for malignant pleural effusion, with tolerable toxic effects. Further study is warranted.

Adolescent↗
PubMed2000

Purification & characterisation of haemolysin from Serratia marcescens B-91.

BACKGROUND & OBJECTIVES: Serratia marcescens an opportunistic human pathogen, is frequently encountered in a variety of debilitating diseases. Relatively little is known about its virulence traits though most clinical isolates secrete a distinct haemolysin which is considered as a useful marker for pathogenicity of Serratia. In this study purification and characterisation of S. marcescens B-91 haemolysin have been attempted. METHODS: S. marcescens B-91 haemolysin was purified to homogeneity from the growth medium using ammonium sulphate fractional precipitation and gel filtration through Sephadex G-75 column. Homogeneity was determined by gel electrophoresis and purified haemolysin was tested for its stability and other characteristics. RESULTS: The haemolysin was characterised to be a 45 kDa molecular weight protein on SDS-polyacrylamide gel electrophoresis. It was inactivated at 60-100 degrees C within 30 min, and on overnight treatment with 2 per cent formaldehyde. It was also susceptible to the action of pronase, protease and trypsin. INTERPRETATION & CONCLUSIONS: The results indicate that the fragile stability of S. marcescens haemolysin is dependent on the storage temperature. The purified haemolysin can be used for understanding the role of haemolysin in the pathogenesis of S. marcescens and also for evaluation of immunoprophylactic activity.

Electrophoresis, Polyacrylamide Gel↗