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PubMed1972

Comparative immunological and enzymatic study of the tryptophan synthetase beta 2 subunit in the Enterobacteriaceae.

The beta(2) subunits of tryptophan synthetase, formula alpha(2)beta(2), from Escherichia coli, Shigella dysenteriae, Enterobacter aerogenes, Salmonella typhimurium, and Serratia marcescens were compared by three criteria. (i) alphabeta association constants for the various beta(2) subunits and E. coli alpha subunit varied between 3.6 x 10(8)m(-1) for E. coli and 0.33 x 10(8)m(-1) for S. marcescens; values for the other organisms were intermediate. (ii) Antiserum neutralization of the beta(2) subunit enzyme activity using anti-E. coli beta(2) serum showed significant cross-reaction among the organisms (E. coli, 1.0; S. dysenteriae, 0.98; S. typhimurium, 0.67; E. aerogenes, 0.61; S. marcescens, 0.42). (iii) Quantitative microcomplement fixation showed E. coli beta(2) and S. marcescens beta(2) subunits to have an index of dissimilarity of 1.8 while the other organisms had intermediate indexes. Similar complement fixation data were obtained with antisera from separate rabbits and from first course and boost sera. These findings suggest that the general surface structure and the respective alpha subunit binding site of the beta(2) subunits from these Enterobacteriaceae have been strongly conserved.

Antigens, Bacterial↗
PubMed1975

Growth rate of Enterobacteriaceae at elevated temperatures: limitation by methionine.

The effect of elevated temperatures on growth rate was studied in five strains of Enterobacteriaceae. In all the strains tested a shift to the elevated temperature resulted in an immediate decrease in growth rate which was due to limitation in the availability of endogenous methionine. The first biosynthetic enzyme of the methionine pathway-homoserine transsuccinylase-was studied in extracts of Aerobacter aerogenes, Salmonella typhimurium, and Escherichia coli and was shown to be temperature sensitive in all of them.

Acyltransferases↗
PubMed1978

Evolution of ribosomal proteins in Enterobacteriaceae.

The evolution of ribosomal proteins of about 70 bacterial strains belonging to the family Enterobacteriaceae has been studied by use of previously reported data (S. Osawa, T. Itoh, and E. Otaka, J. Bacteriol. 107:168-178, 1971) and those obtained in this paper. The proximity of the bacteria was quantified by co-chromatographing the differentially labeled ribosomal proteins from two strains on a column of carboxymethyl cellulose in various combinations. The were then classified into 12 groups (=species?) according to their ribosomal protein compositions and were placed in a phylogenic tree.

Bacterial Proteins↗
PubMed1985

Restriction endonuclease analysis of the ilvGEDA operon of members of the family Enterobacteriaceae.

Four of the genes required for the biosynthesis of isoleucine and valine form the ilvGEDA operon in Escherichia coli K-12 and Salmonella typhimurium. The structural relationship of these genes was examined in eight other members of the family Enterobacteriaceae by genomic Southern blot hybridization. These genes are contiguous in all the strains examined, and specific restriction sites appear to be highly conserved, indicating the possible functional importance of the DNA sequences of which they are part.

Base Sequence↗
PubMed1986

Phosphate-starvation-induced outer membrane proteins of members of the families Enterobacteriaceae and Pseudomonodaceae: demonstration of immunological cross-reactivity with an antiserum specific for porin protein P of Pseudomonas aeruginosa.

Bacteria from members of the families Enterobacteriaceae and Pseudomonadaceae were grown under phosphate-deficient (0.1 to 0.2 mM Pi) conditions and examined for the production of novel membrane proteins. Of the 17 strains examined, 12 expressed a phosphate-starvation-induced outer membrane protein which was heat modifiable in that after solubilization in sodium dodecyl sulfate at low temperature the protein ran on gels as a diffuse band of higher apparent molecular weight, presumably an oligomer form, which shifted to an apparent monomer form after solubilization at high temperature. These proteins fell into two classes based on their monomer molecular weights and the detergent conditions required to release the proteins from the peptidoglycan. The first class, expressed by species of the Pseudomonas fluorescens branch of the family Pseudomonadaceae, was similar to the phosphate-starvation-inducible, channel-forming protein P of Pseudomonas aeruginosa. The second class resembled the major enterobacterial porin proteins and the phosphate-regulated PhoE protein of Escherichia coli. Using a protein P-trimer-specific polyclonal antiserum, we were able to demonstrate cross-reactivity of the oligomeric forms of both classes of these proteins on Western blots. However, this antiserum did not react with the monomeric forms of any of these proteins, including protein P monomers. With a protein P-monomer-specific antiserum, no reactivity was seen with any of the phosphate-starvation-inducible membrane proteins (in either oligomeric or monomeric form), with the exception of protein P monomers. These results suggest the presence of conserved antigenic determinants only in the native, functional proteins.

Antigens, Bacterial↗
PubMed1987

Cloning of genes from members of the family Enterobacteriaceae with mini-Mu bacteriophage containing plasmid replicons.

An in vivo cloning system that uses derivatives of the Escherichia coli bacteriophage Mu with plasmid replicons has been extended to five different species of the family Enterobacteriaceae. Mu and these mini-Mu replicon elements were introduced into strains of E. coli, Shigella flexneri, Salmonella typhimurium, Citrobacter freundii, and Proteus mirabilis by infection, by transformation, or by conjugation with newly constructed broad-host-range plasmids containing insertions of these elements. Lysates from these cells, lysogenic for Mu and mini-Mu elements, were used to infect sensitive recipient strains of E. coli, S. typhimurium, and C. freundii. Drug-resistant transductants had mini-Mu replicon elements with inserts of different DNA sequences. All of the lysogens made could be induced to yield high phage titers, including those coming from strains that were resistant to Mu and Mu derivatives. Clones of 10 particular genes were isolated by their ability to complement specific mutations in the recipient strains, even in the presence of the E. coli K-12 restriction system. Some of the mini-Mu replicon elements used contained lac gene fusing segments and resulted in fusions of the lac operon to control regions in the cloned sequences.

Citrobacter↗
PubMed1991

dGTP triphosphohydrolase, a unique enzyme confined to members of the family Enterobacteriaceae.

The enzyme dGTP triphosphohydrolase (dGTPase; EC 3.1.5.1) was assayed in partially purified extracts of several genera of bacteria, and it was found to be strictly confined to members of the family Enterobacteriaceae. Whereas 11 of 12 enteric bacteria had comparable activity for this enzyme, 8 of 8 nonenteric bacteria, including species in the very closely related genera Vibrio and Aeromonas, did not assay positively for this enzyme. When challenged with Escherichia coli anti-dGTPase antiserum, the active enzymes fell into three groups, retaining 0, approximately 50, or 100% of their original activity. A computer search has revealed an amino acid sequence in the E. coli enzyme which matches well with the single-stranded-DNA binding motif of Prasad and Chiu (J. Mol. Biol. 193:579-584, 1987) and may account for the enzyme's observed interaction with DNA. As far as we are aware, this is the only enzymatic activity so far reported to be present solely in the enteric bacteria.

Amino Acid Sequence↗
PubMed1995

Detection of XerC and XerD recombinases in gram-negative bacteria of the family Enterobacteriaceae.

XerC and XerD are site-specific recombinases of the lambda integrase family which resolve multimeric replicons to monomers by acting at specific sites such as cer, ckr, nmr, parB, and psi, which are found in plasmids, or at the dif site found in the Escherichia coli chromosome. By using Southern hybridizations to cloned E. coli xerC and xerD genes and a cer-nmr plasmid-based resolution assay, the presence of these genes in several species of Enterobacteriaceae is shown.

DNA Nucleotidyltransferases↗
PubMed1997

Coexpression of the long and short forms of CheA, the chemotaxis histidine kinase, by members of the family Enterobacteriaceae.

CheA is the histidine protein kinase of a two-component signal transduction system required for bacterial chemotaxis. Motile cells of the enteric species Escherichia coli and Salmonella typhimurium synthesize two forms of CheA by utilizing in-frame initiation sites within the gene cheA. The full-length protein, CheAL, plays an essential role in the chemotactic signaling pathway. In contrast, the function of the short form, CheAs, remains elusive. Although CheAs lacks the histidine residue that becomes phosphorylated in CheAL, it exhibits both kinase activity and the ability to interact with and enhance the activity of CheZ, a chemotaxis protein that accelerates dephosphorylation of the two-component response regulator CheY. To determine whether other members of the family Enterobacteriaceae express CheAs and CheZ, we analyzed immunoblots of proteins from clinical isolates of a variety of enteric species. All motile, chemotactic isolates that we tested coexpressed CheAL, CheAs, and CheZ. The only exceptions were closely related plant pathogens of the genus Erwinia, which expressed CheAL and CheZ but not CheAs. We also analyzed nucleotide sequences of the cheA loci from isolates of Serratia marcescens and Enterobacter cloacae, demonstrating the presence of in-frame translation initiation sites similar to those observed in the cheA loci of E. coli and S. typhimurium. Since coexpression of CheAs and CheZ appears to be limited to motile, chemotactic enteric bacteria, we propose that CheAs may play an important role in chemotactic responses in some environmental niches encountered by enteric species.

Bacterial Proteins↗
PubMed2001

Intervening sequences in rrl genes and fragmentation of 23S rRNA in genera of the family Enterobacteriaceae.

Intervening sequences (IVSs) in the rrl genes for 23S rRNA are transcribed but later removed by RNase III without religation during RNA processing, leading to fragmented rRNA. We examined about 240 strains of the family Enterobacteriaceae for presence of IVSs using PCR. No IVSs were detected in strains belonging to Escherichia, Shigella, Enterobacter, Erwinia, Ewingella, Hafnia, Kluyvera, Morganella, Pantoea, or Serratia. Previously unreported IVSs were detected in Klebsiella oxytoca, Citrobacter amalonaticus, and Providencia stuartii; previously reported IVSs are in species of Salmonella, Proteus, Providencia, and Yersinia. The sporadic distribution of IVSs indicates lateral genetic transfer of IVSs.

Base Sequence↗
PubMed2006

Direct visualization of red fluorescent lipoproteins indicates conservation of the membrane sorting rules in the family Enterobacteriaceae.

Chimeras created by fusing the monomeric red fluorescent protein (RFP) to a bacterial lipoprotein signal peptide (lipoRFPs) were visualized in the cell envelope by epifluorescence microscopy. Plasmolysis of the bacteria separated the inner and outer membranes, allowing the specific subcellular localization of lipoRFPs to be determined in situ. When equipped with the canonical inner membrane lipoprotein retention signal CDSR, lipoRFP was located in the inner membrane in Escherichia coli, whereas the outer membrane sorting signal CSSR caused lipoRFP to localize to the outer membrane. CFSR-RFP was also routed to the outer membrane, but CFNSR-RFP was located in the inner membrane, consistent with previous data showing that this sequence functions as an inner membrane retention signal. These four lipoproteins exhibited identical localization patterns in a panel of members of the family Enterobacteriaceae, showing that the lipoprotein sorting rules are conserved in these bacteria and validating the use of E. coli as a model system. Although most predicted inner membrane lipoproteins in these bacteria have an aspartate residue after the fatty acylated N-terminal cysteine residue, alternative signals such as CFN can and probably do function in parallel, as indicated by the existence of putative inner membrane lipoproteins with this sequence at their N termini.

Bacterial Proteins↗
PubMed1962

Episome-mediated transfer of drug resistance in Enterobacteriaceae IV. Interactions between resistance transfer factor and F-factor in Escherichia coli K-12.

Watanabe, T. (Keio University, Tokyo, Japan) and T. Fukasawa. Episome-mediated transfer of drug resistance in Enterobacteriaceae. IV. Interactions between resistance transfer factor and F-factor in Escherichia coli K-12. J. Bacteriol. 83:727-735. 1962. - Resistance transfer factor (RTF) present in F(+) and F'(+) strains was found to suppress completely the transfer of F-factor, F', and host chromosomes. On the other hand, the presence of RTF in Hfr strains was found to reduce the frequencies of recombination to about 10(-2) of those in Hfr strains, regardless of the types of Hfr. RTF present in an F(+) strain with colicinogenic factor E(1) inhibited the transfer of the colicinogenic factor, whereas the transfer of colicinogenic factor I was not suppressed by RTF. A hypothesis that the genetic determinant of RTF controlling its "transfer system" is epistatic to that of F-factor is presented. It was also shown that F-factor present in recipients slightly suppresses the acceptance of RTF and that RTF present in recipients slightly reduces the acceptance of F-factor, F', and host chromosomes. On the other hand, the acceptance of RTF by recipients in which RTF is present was found to be about 1% of that in recipients without RTF.

Drug Resistance↗
PubMed1962

Episome-mediated transfer of drug resistance in Enterobacteriaceae. V. Spontaneous segregation and recombination of resistance factors in Salmonella typhimurium.

Watanabe, Tsutomu (Keio University, Tokyo, Japan) and Keong W. Lyang. Episomemediated transfer of drug resistance in Enterobacteriaceae. V. Spontaneous segregation and recombination of resistance factors in Salmonella typhimurium. J. Bacteriol. 84:422-430. 1962.-It was found that spontaneous segregation of the transmissible multiple drug resistance [resistance to streptomycin (Sm), chloramphenicol (Cm), tetracycline (TC), and sulfonamide (Su)] takes place so frequently in Salmonella typhimurium strain LT-2 (Su, Sm, Cm, Tc) as to allow a clone analysis of the segregation of resistance factors with replica plating. Su-, Sm-, and Cm- resistance factors together were spotaneously lost most frequently, whereas the spontaneous loss of Tc-resistance factor alone was rather infrequent. The complete loss of the resistance factors was also noted with low frequencies. The mechanism of the spontaneous segregation of the resistance factors was assumed to be due to either genetic exchange between the resistance factors and host genome or incomplete replication of the transmissible resistance factors (composed of resistance factors and resistance-transfer factor). In relation to the mechanism of spontaneous segregation of the transmissible resistance factors, circular models of the transmissible resistance factors are presented. Four-drug-resistant strains were produced by transferring segregant types of transmissible resistance factors (Su, Sm, Cm) and (Tc) to the strains with (Tc) and (Su, Sm, Cm), respectively. In these four-drug-resistant strains, the two types of transmissible resistance factors were found to be in two different states; in one state the two types of transmissible resistance factors exist in the same cells independently of each other, and in the other state a transmissible resistance factor, which was produced as a result of recombination of the two types of transmissible resistance factors, is present. Two unusual strains of LT-2 with Su-, Sm-, and Cm-resistance factors and with four resistance factors were found. These strains could not transfer their resistance factors to Escherichia coli K-12 by conjugation. Their resistance factors were spontaneously segregated as frequently as those of LT-2 (Su, Sm, Cm) and LT-2 (Su, Sm, Cm, Tc), and the transfer of (Tc) to strain LT-2 with nontransmissible Su-, Sm-, and Cm-resistance factors gave rise to two types of clones; one could transfer the four resistance factors as a unit to K-12 by conjugation, and another could transfer only (Tc) and frequently segregated two types of clones; one had (Tc) and another had nontransmissible Su, Sm-, and Cm-resistance factors. From these findings, the unusual strains with nontransmissible resistance factors are assumed to have a "defective" resistance-transfer factor.

Anti-Bacterial Agents↗
PubMed1964

EXTRACTION AND PURIFICATION OF ENDOTOXIN FROM ENTEROBACTERIACEAE: A COMPARISON OF SELECTED METHODS AND SOURCES.

Fukushi, K. (National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratory, Hamilton, Mont.), R. L. Anacker, W. T. Haskins, M. Landy, K. C. Milner, and E. Ribi. Extraction and purification of endotoxin from Enterobacteriaceae: a comparison of selected methods and sources. J. Bacteriol. 87:391-400. 1964.-Endotoxins containing only 0.2% N (accounted for by amino sugars) and 2% ester- and amide-linked fatty acids (calculated as palmitic acid) were prepared from Salmonella enteritidis. These products were of high biological potency, and were rapidly destroyed by acid hydrolysis. Equally potent acid-susceptible products were derived from different strains of Escherichia coli and Serratia marcescens. No correlation was evident between potency and content of nitrogen, fatty acids, and hexosamine; however, low values for carbohydrate were invariably associated with reduced endotoxic activity. Factors such as strain, method of cultivation, and extraction procedure markedly affected the chemical composition and activity of primary extracts. Results are given which demonstrate significant advantages in the use of cell walls for the isolation and purification of endotoxins.

Carbohydrates↗
PubMed1964

EPISOME-MEDIATED TRANSFER OF DRUG RESISTANCE IN ENTEROBACTERIACEAE. VII. TWO TYPES OF NATURALLY OCCURRING R FACTORS.

Watanabe, Tsutomu (Keio University, Tokyo, Japan), Hiroshi Nishida, Chizuko Ogata, Toshihiko Arai, and Sachiko Sato. Episome-mediated transfer of drug resistance in Enterobacteriaceae. VII. Two types of naturally occurring R factors. J. Bacteriol. 88:716-726. 1964.-Naturally occurring R factors are classified into two types, fi(+) and fi(-), depending on their fi characters. The term fi is an abbreviation of fertility inhibition and fi(-) and fi(-) mean, respectively, the presence and absence of suppression of the functions of the sex factor F of Escherichia coli K-12. It was found that fi(-) R factors reduce the efficiency of plating of phages lambda and T(1) in K-12; fi(+) R factors did not have this inhibitory action. One of the fi(-) R factors reduced the efficiency of plating of phage T(7) as well. Phages lambda and T(1) underwent host-induced modifications in the host carrying some fi(-) R factors. At least two types of fi(-) R factors were recognized by the types of their restriction and host-induced modification of these phages. CaCl(2) exhibited antagonistic actions against the restrictions of phages lambda and T(1) by fi(-) R factors. Transduction of the ability to ferment galactose with HFT lysates of lambda was reduced by fi(-) R factors. Ultraviolet induction of lambda was not affected by any R factors. Furthermore, adsorption of phages lambda and T(1) was not altered by the presence of any R factors. From these results, we concluded that the suppression of progeny formation of these phages by fi(-) R factors is due to some step(s) after adsorption of the phages to the bacteria. Superinfection immunity and mutual exclusion were found between two different fi(+) R factors but not between fi(+) and fi(-) R factors. The two different fi(-) R factors were frequently genetically recombined. but fi(+) and fi(-) R factors were not genetically recombined, as indicated by findings of independent transfer of these R factors by conjugation and by transduction from the donors having these two R factors. It was assumed from these findings that fi(+) and fi(-) R factors are considerably different episomes having different resistance-transfer factors.

Acridines↗
PubMed1964

EPISOME-MEDIATED TRANSFER OF DRUG RESISTANCE IN ENTEROBACTERIACEAE. 8. SIX-DRUG-RESISTANCE R FACTOR.

Watanabe, Tsutomu (Keio University School of Medicine, Tokyo, Japan), Chizuko Ogata, and Sachiko Sato. Episome-mediated transfer of drug resistance in Enterobacteriaceae. VIII. Six-drug-resistance R factor. J. Bacteriol. 88:922-928. 1964.-The multiple-drug-resistant Escherichia coli strain isolated by Lebek in 1963 was found to transfer resistance to sulfonamide, streptomycin, chloramphenicol, tetracycline, kanamycin, and neomycin together by conjugation, as well as by transduction with phage P1kc, suggesting that these drug-resistance markers are carried by a single R factor (R(6)). The results of transductional and spontaneous segregations of the drug-resistance markers of R(6) have shown that R(6) has independent genetic determinants for sulfonamide, streptomycin, chloramphenicol, tetracycline, and kanamycin-neomycin resistance. Resistance to kanamycin and neomycin is probably controlled by a single gene, because no segregation was observed between these two. The resistance transfer factor of R(6) was found to be of the fi(+) type.

Anti-Bacterial Agents↗
PubMed1964

SELECTIVE DESTRUCTION BY PSEUDOMONAS AERUGINOSA OF COMMON ANTIGEN OF ENTEROBACTERIACEAE.

Whang, H. Y. (Children's Hospital, Buffalo, N.Y.), and E. Neter. Selective destruction by Pseudomonas aeruginosa of common antigen of Enterobacteriaceae. J. Bacteriol. 88:1244-1248. 1964.-Supernatant fluids and filtrates from several strains of Pseudomonas aeruginosa, when incubated with common antigen from various enteric bacteria, will produce selective destruction of this antigen, leaving intact the simultaneously present O antigen. This effect is evidenced from hemagglutination, hemolysis, antibody absorption, hemagglutination inhibition, and immunization experiments. The Pseudomonas factor is heat-labile, being destroyed by heating at 100 C for 10 min. The action of this factor on the antigen is time-dependent and temperature-dependent, requiring incubation for 18 to 72 hr and progressing more rapidly at 50 or 56 C than at 37 C. The specificity of the reaction is indicated by the fact that supernatant fluids from cultures of Staphylococcus aureus and Bacillus subtilis, as well as several enzymes, such as pancreatic protease, trypsin, and lipase, have no effect on the common antigen. Utilization of the Pseudomonas factor, conceivably an enzyme, may aid in the eventual elucidation of the chemical nature of the common antigen of enteric bacteria.

Antigens↗
PubMed1965

MUTATIONS TO PENICILLIN RESISTANCE IN THE ENTEROBACTERIACEAE THAT AFFECT SENSITIVITY TO SERUM AND VIRULENCE FOR THE MOUSE.

Roantree, Robert J. (Stanford University School of Medicine, Stanford, Calif.), and John P. Steward. Mutations to penicillin resistance in the Enterobacteriaceae that affect sensitivity to serum and virulence for the mouse. J. Bacteriol 89:630-639. 1965.-Series of mutants resistant to benzylpenicillin or alpha-aminobenzylpenicillin were derived from serum-resistant strains of Escherichia coli and Salmonella by the gradientplate technique. Serum-sensitive mutants were detected in series derived from 16 of the 19 strains used, and these retained the parental O type. Most series were characterized by a mutational step to a high degree of sensitivity to serum. Penicillin-resistant mutants of virulent S. typhimurium and S. enteritidis were less virulent than the parent strains; those which were very sensitive to serum usually showed the greatest loss of virulence. One class of mutants from S. enteritidis was sensitive to human serum but virulent for mice. We found that the mice lack bactericidal antibody against this strain and that immunization with it leads to a high degree of protection.

Ampicillin↗