Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “ENTEROBACTERIACEAE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 343 records · Page 19Linked to original sources

Inducible AmpC beta-lactamase of a new member Enterobacteriaceae.

Extensive biochemical testing and 16S rRNA and rpoB sequence analysis revealed that clinical strain CF01Ent1, initially identified as Buttiauxella agrestis by the use of Api 32 biochemical strips, is a new organism in the Enterobacteriaceae family. It produced an inducible AmpC-type beta-lactamase whose sequence shares 69 to 72% identity with those of the other AmpC-type beta-lactamases of ENTEROBACTERIACEAE: This enzyme exhibits an atypical high affinity for all beta-lactams tested.

Amino Acid Sequence↗

Differentiation of selected Enterobacteriaceae by pyrolysis-gas-liquid chromatography.

Pyrolysis-gas-liquid chromatography was used to differentiate selected species of Enterobacteriaceae. Individual cultures of Salmonella typhi, Hafnia alvei, and Proteus vulgaris, and 12 strains of Yersinia enterocolitica were grown in nutrient broth. After harvest and lyophilization, the bacterial samples were pyrolyzed at 900 degrees C, and their volatile fractions were separated on a 50-m capillary column coated with Carbowax 20M. The resulting pyrolysis elution patterns (pyrograms) of the four species were monitored on an integrating console, which was coupled with the chromatographic detector. The pyrograms were divided into 312 30-s time interval areas, and each interval area was normalized in relation to the area of the entire curve. The normalized areas were evaluated by stepwise linear discriminant analysis, and the discriminating component coordinates were used to generate a plot of the canonical variables. Distinct clustering patterns allowed discrimination among the four genera of Enterobacteriaceae studied. The tight clustering of the 12 Y. enterocolitica strains suggests the advantage of pyrolysis-gas-liquid chromatography over traditional approaches for species identification.

Bacteriological Techniques↗

Enterobacteriaceae and Aeromonas hydrophila in Minnesota frogs and tadpoles (Rana pipiens).

In 222 Rana pipiens frogs and 34 tadpoles captured in and near Minnesota, Aeromonas hydrophila and 29 species of Enterobacteriaceae, including yersinia enterocolitica and Salmonella arizonae, were isolated from intestines. The prevalence of members of the family Enterobacteriaceae was lowest in frogs captured in early spring and highest in frogs captured in late summer.

Aeromonas↗

Identification of members of the family Enterobacteriaceae by the R-B system.

The R-B system was evaluated in parallel with conventional bacteriological procedures for the identification of members of the family Enterobacteriaceae by using bacterial strains from a variety of clinical specimens and from stock cultures. The R-B tests found to be reliable were, in decreasing order, the reactions for phenylalanine deaminase, hydrogen sulfide, and indole, the production of gas from glucose, and the decarboxylation of ornithine. The reactions in the R-B system found to be unreliable were motility, the decarboxylation of lysine, and the fermentation of both glucose and lactose. In addition, the reactions of the R-B system were more difficult to read and interpret than those of the conventional system. On the basis of this evaluation, it was concluded that the R-B system is not an acceptable alternative to the conventional methods in the identification of the Enterobacteriaceae.

Bacteriological Techniques↗

Comparison of conventional methods, the R-B system, and modified R-B system as guides to the major divisions of Enterobacteriaceae.

Primary grouping of more than 2,000 members of Enterobacteriaceae, freshly isolated from clinical specimens, was performed on the basis of eight conventional laboratory tests used routinely in this laboratory and by the R/B system. Results indicate that both systems perform well in this first step in the identification of various medically significant species of the family. Difficulties encountered with certain reactions of the R/B system were corrected with a physical modification of the tubes. An additional 100 representatives of Enterobacteriaceae were compared with conventional methods and the modified R/B system. Results indicate improvement in observing and interpreting findings with the R/B system.

Aminohydrolases↗

Catalase test as an aid to the identification of Enterobacteriaceae.

Although the catalase test has been used for many years for rapid differentiation of the genera of gram-positive organisms, little has been said about its use in the family Enterobacteriaceae. It was further noted that a wide variety of methods exist for the execution of the catalase test, that there is no universally accepted strength specified for the hydrogen peroxide, and that no gradations for the vigor and speed of the reaction have been mentioned. Under the conditions of the clinical laboratory, we have developed a simple, rapid, and accurate method for the catalase test that has been of great value as an aid in the identification of the Enterobacteriaceae. With 3% H(2)O(2), it was observed that Serratia, Proteus, and Providencia were vigorous catalase reactors. Only Salmonella and rare Escherichia, Enterobacter, and Klebsiella isolates were moderate catalase reactors. Escherichia and Shigella strains were mostly nonreactive, with less than one-third weekly (+) reactive, whereas most Enterobacter strains tended to be weakly reactive. Klebsiella strains were divided equally between nonreactive and weakly reactive. In practice, this test was also of great value in discerning nonpigmented Serratia cultured from the hospital environment and in detecting mixed flora containing nonspreading Proteus.

Bacteriological Techniques↗

r-b Expanders: their use in identifying routinely and unusually reacting members of Enterobacteriaceae.

This cooperative study between a large clinical laboratory and a reference laboratory evaluated the performance of the expanded r/b system for identifying Enterobacteriaceae. The 2,200 cultures isolated in the normal hospital routine presented no problem of identification to the r/b system. About 250 "atypical" cultures which were exchanged between the collaborating laboratories were also identified accurately. The expanded r/b system was found to perform as well as most biochemical-physiological identification systems, and when used appropriately was highly satisfactory as a system for identification of Enterobacteriaceae.

Arabinose↗

Evaluation of the Minitek system for identification of Enterobacteriaceae.

Clinical isolates (869) and stock cultures (35) of Enterobacteriaceae were tested in parallel with the Minitek and conventional systems. The Minitek correctly identified 822 of 904 cultures. When a deoxyribonuclease plate was inoculated along with the Minitek, it was possible to speciate Enterobacteriaceae within 24 h. False-positive hydrogen sulfide reactions were the major fault with this system. Reactions were clear-cut and easy for technologists to read.

Bacteriological Techniques↗

Evaluation of the BBL Minitek system for the identification of Enterobacteriaceae.

Thirty-one different substrate disks were tested in parallel with comparable, prepared media (BBL) against a minimum of 300 cultures of Enterobacteriaceae. An overall correlation of 98% was observed with all the disks tested. In addition, the system was used to identify 461 fresh isolates of Enterobacteriaceae in parallel with conventional media using the schema used at the Veterans Administration Hospital, Baltimore. An overall correlation of 97% was observed. Minitek is a time and space saving system. It is accurate and easily adapted to the clinical laboratory. A wide variety of substrates are available, allowing most laboratories to use their own schema. The long shelf life of most disks is a definite advantage.

Bacteriological Techniques↗

Conservation of transfer ribonucleic acid and 5S ribonucleic acid cistrons in Enterobacteriaceae.

The genes for tranfer ribonucleic acid (tDNA) and 5S ribonucleic acid (5SDNA) were isolated from the total deoxyribonucleic acid (DNA) of Escherichia coli. The relatedness of tDNA and 5S from E. coli and other species of Enterobacteriaceae was determined by reassociation of the isolated genes labeled with 32PO4 to unlabeled, unfractionated DNA. Double-stranded DNA was separated from unreacted DNA by hydroxyapatite chromatography. Thermal elution profiles were done to determine the amount of unpaired bases present in related DNA sequences. Relative to total DNA, both 5S DNA and tDNA were highly conserved throughout the Enterobacteriaceae, including the genera Yersinia and Proteus.

DNA, Bacterial↗

Immunochemical comparison of phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase among the Enterobacteriaceae.

The bifunctional enzyme of the tryptophan operon, phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase (PRAI-InGPS;EC 4.1.1.48), was characterized by an immunochemical study of six representative members of the Enterobacteriaceae: Escherichia coli, Salmonella typhimurium, Enterobacter aerogenes, Serratia marcescens, Erwinia carotovora, and Proteus vulgaris. PRAI-InGPS was purified from E. coli, and antisera were prepared in rabbits. These antisera were utilized in quantitative microcomplement fixation allowing for a comparison of the overall antigenic surface structure of the various homologous enzymes. These data showed E. coli PRAI-InGPS and S. marcescens and E. carotovora PRAI-InGPS (taken as a group) to have an index of dissimilarity of approximately 10, whereas the other organisms had values intermediate. In addition, antiserum to E. coli tryptophan synthetase beta2 subunit was used in microcomplement fixation to extend the previous comparison of this subunit (Rocha, Crawford, and Mills, 1972) to E. carotovora and P. vulgaris. Indexes of dissimilarity for E. coli compared to P. vulgaris of E. carotovora were 1.0 and 1.7, respectively. Agar immunodiffusion using PRAI-Ingps antisera showed significant cross-reaction among E. coli, E. aerogenes, S. typhimurium, and P. vulgaris whereas the enzymes from S. marcescens and E. carotovora cross-reacted to a lesser extent, with the latter reaction being quite weak. Comparative enzyme neutralization using E. coli PRAI-InGPS antisera showed significant cross-reactions among the enzymes in that all were neutralized at least 25%. The data taken together indicate that the trpC gene products in the Enterobacteriaceae are a homologous group of proteins, that the genetic divergene of the trpC gene is basically the same as the trpA gene, and that both are less conserved than the trpB gene. Furthermore, the PRAI-InGPS, enzyme active site appears to represent a more evolutionarily conserved region of the protein. These findings indicate that, with respect to PRAI-InGPS, similarity to E. coli among the organisms examined is in the following order: (E. aerogenes, S. typhimurium, P. vulgaris) greater than (S. marcescens, E. carotovora).

Antigens, Bacterial↗

Comparative immunological studies on arylsulfatase in bacteria of the family Enterobacteriaceae: occurrence of latent arylsulfatase protein regulated by sulfur compounds and tyramine.

The arylsulfatases of 21 strains of the family Enterobacteriaceae were compared by measuring their enzymatic activities and immunological reactivities. Enzyme formation under repressing, nonrepressing, and derepressing conditions was tested. Antiserum prepared against pure arylsulfatase from Klebsiella aerobgenes W70 was tested against the enzyme extracts from the strains using double diffusion, quantitative precipitation, and immunoelectrophoresis. No close relationship was found between arylsulfatase activity and immunological cross-reactionship was found between arylsulfatase activity and immunological cross-reactivity. The strains in the family Enterobacteriaceae could be divided into two groups on the basis of the immunological properties of their enzyme. Antisera formed a precipitin band with both active and inactive enzyme proteins from Escherichia, Citrobacter, Salmonella, Klebsiella, and Enterobacter, but not with the proteins from Serratia, Proteus, and Erwinia, even though some strains of these species had enzyme activity. It was also found that the formation of arylsulfatase proteins, irrespective of whether they had enzyme activity, were under regulation by sulfur compounds and tyramine.

Arylsulfatases↗

Frequency among Enterobacteriaceae of the DNA sequences encoding type 1 pili.

Type 1 pili, characterized by mannose-inhibitable agglutination of fowl or guinea pig erythrocytes, have been found throughout the family Enterobacteriaceae. A radiolabeled probe was prepared from a restriction endonuclease-digested fragment of the Escherichia coli pil operon and used to detect homologous DNA sequences in 236 bacteria representing 11 genera of Enterobacteriaceae. Only isolates identified as E. coli or Shigella spp. exhibited homology. In contrast, mannose-sensitive hemagglutination was observed in nine genera. Probe DNA did not hybridize to plasmid DNA, indicating a chromosomal location for the pil operon. Analysis of restriction nuclease-digested whole-cell DNA from 60 E. coli and two Shigella sp. isolates indicated that internal sequences were conserved in most strains, but that changes in flanking sequences in the chromosome were common.

DNA Restriction Enzymes↗

Antigenic polymorphism of the LamB protein among members of the family Enterobacteriaceae.

In this study we demonstrate that most members of the family Enterobacteriaceae possess a maltose-inducible outer membrane protein homologous to the LamB protein of Escherichia coli K-12. These proteins react with polyclonal antibodies raised against the LamB protein of E. coli K-12. We compared the antigenic structure of the LamB protein in members of the family Enterobacteriaceae with six monoclonal antibodies raised against the LamB protein of E. coli K-12. Four of them reacted with epitopes located at the outer face of the membrane, and two reacted with epitopes located at the inner face of the membrane. A great degree of variability was observed for the external epitopes. Even in a single species, such as E. coli, an important polymorphism was present. In contrast, the internal epitopes were more conserved.

Antigens, Bacterial↗

In vivo formation of hybrid aspartate transcarbamoylases from native subunits of divergent members of the family Enterobacteriaceae.

The genes encoding the catalytic (pyrB) and regulatory (pyrI) polypeptides of aspartate transcarbamoylase (ATCase, EC 2.1.3.2) from several members of the family Enterobacteriaceae appear to be organized as bicistronic operons. The pyrBI gene regions from several enteric sources were cloned into selected plasmid vectors and expressed in Escherichia coli. Subsequently, the catalytic cistrons were subcloned and expressed independently from the regulatory cistrons from several of these sources. The regulatory cistron of E. coli was cloned separately and expressed from lac promoter-operator vectors. By utilizing plasmids from different incompatibility groups, it was possible to express catalytic and regulatory cistrons from different bacterial sources in the same cell. In all cases examined, the regulatory and catalytic polypeptides spontaneously assembled to form stable functional hybrid holoenzymes. This hybrid enzyme formation indicates that the r:c domains of interaction, as well as the dodecameric architecture, are conserved within the Enterobacteriaceae. The catalytic subunits of the hybrid ATCases originated from native enzymes possessing varied responses to allosteric effectors (CTP inhibition, CTP activation, or very slight responses; and ATP activation or no ATP response). However, each of the hybrid ATCases formed with regulatory subunits from E. coli demonstrated ATP activation and CTP inhibition, which suggests that the allosteric control characteristics are determined by the regulatory subunits.

Adenosine Triphosphate↗

Identification of TonB homologs in the family Enterobacteriaceae and evidence for conservation of TonB-dependent energy transduction complexes.

The transport of Fe(III)-siderophore complexes and vitamin B12 across the outer membrane of Escherichia coli requires the TonB-dependent energy transduction system. A set of murine monoclonal antibodies (MAbs) was generated against an E. coli TrpC-TonB fusion protein to facilitate structure and function studies. In the present study, the epitopes recognized by these MAbs were mapped, and their distribution in gram-negative organisms was examined. Cross-species reactivity patterns obtained against TonB homologs of known sequence were used to refine epitope mapping, with some epitopes ultimately confirmed by inhibition experiments using synthetic polypeptides. Epitopes recognized by this set of MAbs were conserved in TonB homologs for 9 of 12 species in the family Enterobacteriaceae (including E. coli), including previously unidentified TonB homologs in Shigella, Citrobacter, Proteus, and Kluyvera species. These homologs were also detected by a polyclonal alpha-TrpC-TonB serum that additionally recognized the known Yersinia enterocolitica TonB homolog and a putative TonB homolog in Edwardsiella tarda. These antibody preparations failed to detect the known TonB homologs of either Pseudomonas putida or Haemophilus influenzae but did identify potential TonB homologs in several other nonenteric gram-negative species. In vivo chemical cross-linking experiments demonstrated that in addition to TonB, auxiliary components of the TonB-dependent energy transduction system are broadly conserved in members of the family Enterobacteriaceae, suggesting that the TonB system represents a common system for high-affinity active transport across the gram-negative outer membrane.

Amino Acid Sequence↗

Episome-mediated transfer of drug resistance in Enterobacteriaceae. III. Transduotion of resistance factors.

Watanabe, Tsutomu (Keio University, Tokyo, Japan), and Toshio Fukasawa. Episome-mediated transfer of drug resistance in Enterobacteriaceae. III. Transduction of resistance factors. J. Bacteriol. 82:202-209. 1961.-Transmissible multiple drug resistance of Enterobacteriaceae, which includes resistance to streptomycin (SM), chloramphenicol (CM), tetracycline (TC), and sulfonamide (Su), was found to be transduced in the systems of Salmonella typhimurium strain LT-2 with phage P-22 and Escherichia coli strain K-12 with phage P1kc. No linked chromosomal markers to the resistance factors have so far been found in the substrains of K-12. The transductants of K-12 were all found to be able to transfer their resistance factors by conjugation, whereas a majority of those of LT-2 could not transfer their resistance factors by conjugation. The resistance factors were segregated rarely in K-12 and consistently in LT-2. Defective resistance factors could be transferred by conjugation to the transductants of LT-2. The transductants thus made resistant to the four drugs were able to transfer only the resistance factors which had been introduced by conjugation and none of those which had been transduced. The patterns of segregation of the resistance factors by transduction suggested that they are located in the following sequence; Su-----Sm-----Cm-----Tc, and they were assumed to be carried by an episome "resistance transfer factor" which is considered to be located at the distal end of Tc.

Anti-Bacterial Agents↗