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PubMed1972

Numerical diagnostic key for the identification of Enterobacteriaceae.

A numerical diagnostic key for enteric organisms is described which permits the identification of typical strains and of biochemical variants with high accuracy. Unknown strains are inoculated into a basic set of five media which permit the testing of eight biochemical reactions. The positive reactions are assigned points, and the score of a strain is added up, after which the identification of the strain is obtained from a table. In many instances, the final identification is obtained with this set of biochemical tests; and, in other instances, a small number of additional tests are required to distinguish between organisms giving the same score in the basic set of biochemical tests. The key permits an accurate, rapid, and economical differentiation of the typical and the more common atypical biotypes of enteric organisms in the clinical laboratory.

Culture Media↗
PubMed1972

Rapid ornithine decarboxylase test for the identification of enterobacteriaceae.

Conventional methods for detecting ornithine decarboxylase activity require an extended period of incubation. However, with a few simple modifications, accurate results were obtained within a few hours rather than several days. The broth medium was modified, primarily by omitting glucose and by decreasing the pH to 5.5. A 1-ml amount of this broth was inoculated with one colony and then overlaid with sterile mineral oil. Within 2 to 4 hr, the pH increased if ornithine was decarboxylated, thus changing the color of the internal pH indicator to a dark purple. If the amino acid was not decarboxylated, the pH decreased to pH 5.0 to 5.2, enough to give a definite yellow color. With 347 selected clinical isolates, the rapid test gave results identical to those obtained in 1 to 4 days with Moeller's decarboxylase medium. Less reliable results were obtained with Difco's decarboxylase medium with 0.3% agar which was stabinoculated and read after 18 to 24 hr without a mineral oil seal. The rapid ornithine decarboxylase test represents a simple, accurate technique which is well suited for the clinical microbiology laboratory.

Bacteriological Techniques↗
PubMed2005

Manual and automated instrumentation for identification of Enterobacteriaceae and other aerobic gram-negative bacilli.

Identification of gram-negative bacilli, both enteric and nonenteric, by conventional methods is not realistic for clinical microbiology laboratories performing routine cultures in today's world. The use of commercial kits, either manual or automated, to identify these organisms is a common practice. The advent of rapid or "spot" testing has eliminated the need for some commonly isolated organisms to be identified with the systems approach. Commercially available systems provide more in-depth identification to the species level as well as detect new and unusual strains. The answers obtained from these systems may not always be correct and must be interpreted with caution. The patient demographics, laboratory workload and work flow, and technologist's skill levels should dictate the system of choice. Cost considerations introduce another variable into the equation affecting choice. Each system has its own strengths and weaknesses, and each laboratory must decide on the level of sophistication that fulfills its particular needs.

Automation↗
PubMed1976

Strain-related differences in immunosuppressive effects of Enterobacteriaceae and their lipopolysaccharides on production in rabbits of antibody to enterobacterial common antigen.

Certain polysaccharides have been shown to inhibit the antibody response of rabbits to the common enterobacterial antigen (CA). The present investigation revealed that striking differences exist in the immunosuppressive effects of enteric bacteria and their lipolysaccharides (lps), depending upon CA production by the strains. Mixtures of immunogenic strains (Escherichia coli F2378 [R4], E. coli F470 [R1], or Shigella boydii F3140 [R]) and non-immunogenic CA-producing strains, such as E. coli O1, E. coli O113, Salmonella montevideo, and S. minnesota, as well as the R mutants E. coli F614 (R1), E. coli F757 (R1), and S. typhimurium his 642 (Ra), failed to elicit CA antibodies. In contrast, mixtures of the immunogen and CA-negative strains S. typhimurium his 386 (Ra) and S. minnesota P595 (Re) or R555 (Ra) yielded antibodies in titers similar to those elicited by the immunogen alone. Further, LPS of CA-positive but not of CA-negative strains exerted this immunosuppressive effect. Quantitative studies revealed that LPS of S. minnesota in amounts of 100 mug/ml was strongly immunosuppressive, in amounts of 20 mug/ml slightly effective, and in amounts of 4 mug/ml ineffective. It is postulated that hitherto unknown differences exist, either in composition or in configuration, between LPS obtained from different microorganisms to account for the strain-related differences in immunosuppressive effects and, further, that the immunosuppressive LPS interacts with immunogenic CA.

Animals↗
PubMed1983

Synthesis of plasmid-coded heat-labile enterotoxin in wild-type and hypertoxinogenic strains of Escherichia coli and in other genera of Enterobacteriaceae.

The effect of host determinants on expression of plasmid-coded heat-labile enterotoxin (LT) was examined. A collection of LT plasmids was introduced into isogenic strains of Escherichia coli K-12 strains containing the wild type or hypertoxinogenic (htx-2) allele. For each plasmid tested, production of LT increased by approximately 1.5- to 3-fold in the host containing htx-2, indicating that the htx-2 allele affects a regulatory function for LT production that is common to many different enterotoxin plasmids. LT plasmids from E. coli were also introduced into strains of Shigella flexneri, Shigella sonnei, Citrobacter freundii, Enterobacter cloacae, Klebsiella pneumoniae, and Salmonella typhimurium. The plasmids were stably maintained and determined production of LT in those genera, although the amounts of LT produced varied by more than 50-fold. These observations demonstrate that host factors have an important role in determining the level of expression of plasmid-coded LT genes and support the hypothesis that interspecific, conjugal transfer of enterotoxin plasmids may confer enterotoxigenicity to a wide variety of potentially pathogenic enteric bacteria.

Alleles↗
PubMed1985

Construction and comparison of recombinant plasmids encoding type 1 fimbriae of members of the family Enterobacteriaceae.

The genes encoding type 1 fimbriae of Salmonella typhimurium, Enterobacter cloacae, and Serratia marcescens were cloned in Escherichia coli. All transformants possessing recombinant plasmids were shown to be fimbriate and demonstrated mannose-sensitive hemagglutinating activity. A comparison of the physical maps of these plasmids revealed little similarity among them, although plasmids encoding type 1 fimbriae of Escherichia coli and Klebsiella pneumoniae appeared similar with respect to restriction enzyme sites. The fimbrial gene cluster ranged in size from 5.5 to 9.0 kilobase pairs as determined by transposon mutagenesis. Plasmid-containing E. coli strains were shown to produce species-specific fimbrial antigens with little or no cross-reactivity between genera. Therefore, it was presumed that each plasmid contained the gene encoding the fimbrial subunit. Complementation was not detected between nonfimbriate insertion mutants of different species but was seen with mutants of the same species.

Antigens, Bacterial↗
PubMed1985

Complementation analyses of recombinant plasmids encoding type 1 fimbriae of members of the family Enterobacteriaceae.

Insertion mutants of recombinant plasmids encoding type 1 fimbriae of four genera of enteric bacteria were used to detect genetic complementation. After transformation by pairs of plasmids, double transformants were screened for their ability to express type 1 fimbriae. Complementation was observed between genes derived from the same genus but was absent with chimeric molecules carrying genetic information from two different genera. The results indicate that diffusible gene products of the fim cluster are necessary for phenotypic expression of type 1 fimbriae.

Adhesiveness↗
PubMed1986

Lipopolysaccharide structures in Enterobacteriaceae, Pseudomonas aeruginosa, and Vibrio cholerae are immunologically related to Campylobacter spp.

To determine whether lipopolysaccharide (LPS) structures of Campylobacter species are immunologically related to those of 11 other gram-negative organisms, we immunoblotted from polyacrylamide gels the LPS of these strains with immune rabbit serum raised against six Campylobacter jejuni strains and two Campylobacter fetus strains. The LPS studied were from Salmonella minnesota wild type and Ra to Re mutants, Salmonella typhi, Escherichia coli, Yersinia enterocolitica, Vibrio cholerae, and Pseudomonas aeruginosa. None of the 11 LPS preparations was recognized by the eight antisera, but antisera to each of the Campylobacter strains recognized core determinants of some LPS preparations. Antiserum directed against the most serum-sensitive C. jejuni strain, 79-193, was the only antiserum sample that recognized core regions of the rough Salmonella mutants. In converse experiments, when LPS preparations from five Campylobacter strains were blotted with antiserum to Salmonella lipid A, recognition of core structures of each was shown; data from an enzyme-linked immunosorbent assay confirmed this result. In contrast, antiserum to Salmonella typhimurium Re LPS showed no reactivity. We conclude that LPS of Campylobacter strains share lipid A antigenic determinants with the core region of LPS of several other gram-negative organisms.

Campylobacter↗
PubMed1997

Immunomodulatory properties of porins of some members of the family Enterobacteriaceae.

The outer membrane protein (OMP) preparation of Salmonella typhi was observed to have several immunomodulatory properties. Treatment of mice with an intraperitoneal injection of the OMP preparation enhanced both cellular and humoral responses of the mice to an unrelated antigen, a killed vaccine of Mycobacterium vaccae; both the delayed-type hypersensitivity (DTH) response and the antibody titers were enhanced. The predominant isotype of the antibody shifted from immunoglobulin G1 (IgG1) to IgG2a upon treatment with OMP. Treatment of mice with the OMP preparation improved the efficiency of in vitro antigen presentation by the peritoneal cells and also induced the cells to secrete interleukin-1. Treatment with the lipopolysaccharide (LPS) preparation of S. typhi had the opposite effect; i.e., the DTH response to M. vaccae was suppressed. Treatment with OMP neutralized the suppressive effects of LPS. The OMP preparation also had an enhancing effect on the innate immune mechanisms of the mice. Intraperitoneal injection of the OMP preparation enhanced the microbicidal activity of the peritoneal cells, and production of nitric oxide intermediates was stimulated. Injection of the OMP preparation into footpads of naive nonimmune mice induced a sustained hypersensitivity response that peaked at 24 h. Purified porins of the OMP preparation could induce both immunomodulation and hypersensitivity. Porins prepared from five different Salmonella strains and a strain of normal fecal Escherichia coli also exhibited immunomodulatory and hypersensitivity-inducing activities.

Adjuvants, Immunologic↗
PubMed2003

Production of cellulose and curli fimbriae by members of the family Enterobacteriaceae isolated from the human gastrointestinal tract.

Citrobacter spp., Enterobacter spp., and Klebsiella spp. isolated from the human gut were investigated for the biosynthesis of cellulose and curli fimbriae (csg). While Citrobacter spp. produced curli fimbriae and cellulose and Enterobacter spp. produced cellulose with various temperature-regulatory programs, Klebsiella spp. did not show pronounced expression of those extracellular matrix components. Investigation of multicellular behavior in two Citrobacter species and Enterobacter sakazakii showed an extracellular matrix, cell clumping, pellicle formation, and biofilm formation associated with the expression of cellulose and curli fimbriae. In those three strains, the csgD-csgBA region and the cellulose synthase gene bcsA were conserved. PCR screening for the presence of csgD, csgA and bcsA revealed that besides Klebsiella pneumoniae and Klebsiella oxytoca, all species investigated harbored the genetic information for expression of curli fimbriae and cellulose. Since Citrobacter spp., Enterobacter spp., and Klebsiella spp. are frequently found to cause biofilm-related infections such as catheter-associated urinary tract infections, the human gut could serve as a reservoir for dissemination of biofilm-forming isolates.

Amino Acid Sequence↗
PubMed1975

Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes.

Several physical properties of the first four enzymatic activities of the tryptophan pathway were examined using gel filtration and ion exchange chromatography. Five different patterns were noted. Differences in the anthranilate synthetase (AS) and phosphoribosylanthranilate transferase (PRT) defined these patterns. In all the organisms studied phosphoribosylanthranilate isomerase and indoleglycerol phosphate synthetase co-eluted from both diethylaminoethyl-cellulose and G-200 and thus probably are contained in a single polypeptide of 50,000 daltons. An AS-PRT complex was found in Citrobacter species, Enterobacter cloacae, and Erwinia dissolvens. In all the other bacteria examined AS and PTR were separate molecules. In Serratia marcescens, S. marinorubra, and Enterobacter liquefaciens, AS was 140,000 daltons and PRT was 45,000 daltons. In Erwinia carotavora and Enterobacter hafniae the AS was the same size as the Serratia species but the PRT was larger at 67,000 daltons. Two Proteus species had an AS and PRT of the same size as E. carotavora and E. halfniae but the Proteus AS was different in that it partially dissociated upon gel filtration. Aeromonas formicans was unique in its possession of an AS with a molecular weight of 220,000. The PRT of A. formicans was found to elute at 67,000 daltons. Possible paths of evolution of the tryptophan enzymes are discussed in terms of the results of this study. The results presented here are also considered with respect to existing taxonomic schemes of the enteric bacteria.

Anthranilate Synthase↗
PubMed1978

Trypsin peptide patterns of tryptophan synthase beta2 protein among four species of the Enterobacteriaceae.

The tryptophan synthase beta 2 protein (EC 4.2.1.20) of Escherichia coli, Enterobacter aerogenes, Serratia marcescens, and Erwinia carotovora was purified and compared. Two-dimensional total peptide patterns for each of the four beta2 proteins obtained after digestion with trypsin showed that approximately three quarters of the total peptides are common to all four peptides. Examination of only arginine-containing peptides showed that approximately half of these peptides are common. From a comparative standpoint, the data provide evidence that the primary structure of beta 2 proteins is relatively similar, indicating that the trpB cistron is evolutionarily conserved in the enteric bacteria group.

Bacterial Proteins↗
PubMed1987

Frequency of IS1-mediated molecular events in different members of the family Enterobacteriaceae.

The numbers of chromosomal copies of the insertion sequence IS1 in strains of Salmonella typhimurium (0 to 8 copies), Shigella sonnei (56 copies), and Shigella flexneri (41 copies) isolated in Mexico City, Mexico, were similar to those reported for these genera isolated in other countries. Of the 11 Shigella strains studied, all carried several small plasmids; however, in only one of these strains did a small plasmid contain IS1, IS1 recombination, cointegrate formation mediated by IS1 or by the IS1-flanked transposon Tn9, and transposition of Tn9 occurred at a higher frequency in S. typhimurium than in either Escherichia coli or S. sonnei strains. The frequencies of IS1 recombination in S. typhimurium strains containing either zero or eight copies of IS1 were similar.

DNA Transposable Elements↗
PubMed1989

Phosphate regulon in members of the family Enterobacteriaceae: comparison of the phoB-phoR operons of Escherichia coli, Shigella dysenteriae, and Klebsiella pneumoniae.

The structure and function of the phoB and phoR genes of Shigella dysenteriae strains and Klebsiella pneumoniae, which are involved in regulation of the phosphate regulon, were analyzed. Complementation tests among the genes of Escherichia coli, S. dysenteriae strains, and K. pneumoniae for production of alkaline phosphatase indicate that S. dysenteriae serotype 2 and serotype 3 strains and K. pneumoniae are phoA+ phoB+ phoR+ but S. dysenteriae Sh and serotype 1 strains are phoA phoB+ phoR. Nucleotide sequences of phoB and phoR of S. dysenteriae Sh and K. pneumoniae are highly homologous to those of E. coli, except for a single base insertion found in phoR of S. dysenteriae Sh.

Alkaline Phosphatase↗
PubMed1993

The plasmid-encoded urease gene cluster of the family Enterobacteriaceae is positively regulated by UreR, a member of the AraC family of transcriptional activators.

Ureolytic clinical isolates of Providencia stuartii, Salmonella spp., and some Escherichia coli strains contain large urease-encoding plasmids. Expression of urease activity from these isolates is induced at least 20-fold by urea. In order to facilitate studies on the regulatory mechanism controlling this urea-inducible expression, the plasmid-encoded urease genes were inserted into the low-copy-number vector pRK415, to form pSEF70. Deletion mutagenesis of pSEF70 demonstrated that between 1.3 and 1.6 kb of DNA upstream of ureD (the first of seven urease genes clustered in an operon-like fashion) was required for a urease-positive phenotype. An open reading frame coding for a 34.1-kDa polypeptide was found in the DNA sequence of this upstream region. This open reading frame has been designated ureR, for urease regulator. A urea-inducible promoter region was identified upstream of ureD. Transcription from this promoter was activated only when ureR was present in trans. The predicted ureR gene product contains a helix-turn-helix motif and shows significant amino acid similarity to the AraC family of transcriptional activators. We conclude that urea-dependent expression from the plasmid-encoded urease gene cluster requires ureR and that ureR codes for a positive regulatory element controlling transcription of at least one essential urease gene, ureD.

Amino Acid Sequence↗