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At least 19 recordsLinked to original sources

PubMed1963

FOLIC ACID DERIVATIVES SYNTHESIZED DURING GROWTH OF DIPLOCOCCUS PNEUMONIA.

Sirotnak, F. M. (Sloan-Kettering Institute for Cancer Research, New York, N.Y.), Gloria J. Donati, and Dorris J. Hutchison. Folic acid derivatives synthesized during growth of Diplococcus pneumoniae. J. Bacteriol. 85:658-665. 1963.-Under cultural conditions permitting synthesis of folic acid in an amount greatly in excess (20- to 30-fold) of that required for maximal growth of Diplococcus pneumoniae, 85 to 90% of the growth factor accumulated as polyglutamates. Approximately equal amounts of mono- and diglutamates made up the remaining 10 to 15% found in culture material. Most of the polyglutamates occurred intracellularly, in a proportion of triglutamates to higher glutamates of about two to one. Only 10 to 15% of all folic acid derivatives (mono-, di-, and polyglutamates) found had folinic acid (5-formylfolate-H(4)) activity for Pediococcus cerevisiae. Practically all synthesis of the glutamyl-peptide moieties of folate seems to occur at an enzymatic step prior to folic acid, since no appreciable peptide formation occurred under conditions blocking folate synthesis. Sulfanilamide inhibition of growth by a block in folate synthesis was reversed by the addition of dihydrofolic acid, but not folic acid. The examination of two genetically distinct amethopterin-resistant mutant strains has revealed no gross differences in folate accumulation during growth when compared with the wild strain.

Antimetabolites↗

PubMed1963

ALTERATION IN TRANSFORMABILITY OF DIPLOCOCCUS PNEUMONIAE AFTER THE ACQUISITION OF GENETIC DETERMINANTS INDUCING RESISTANCE TO ERYTHROMYCIN.

Sirotnak, Francis M. (Sloan-Kettering Institute for Cancer Research, New York, N.Y.), Ramona B. Lunt, and Dorris J. Hutchison. Alteration in transformability of Diplococcus pneumoniae after the acquisition of genetic determinants inducing resistance to erythromycin. J. Bacteriol. 86:735-739. 1963.-The genetic alteration of a highly transformable (competent) recipient strain of Diplococcus pneumoniae by the transformation of at least two of three identified erythromycin-resistance determinants (Ery(a), Ery(b), Ery(c)) results in a marked decrease (Ery(a-b) recombinant) or complete loss (Ery(a-c) recombinant) in the ability to be transformed. The occurrence of transformable cells in cultures of the R6 Ery(a-b) recombinant strains, although greatly diminished, still varies during growth in a manner characteristic of the fully competent parent strain. Both Ery(b) and Ery(c) determinants appear to be linked to Ery(a). In experiments using P(32)-labeled deoxyribonucleic acid (DNA), data correlating DNA uptake with transformation show a decrease or loss in uptake capacity of the erythromycin-resistant strains.

DNA↗

PubMed1962

Intermediary metabolism of Diplococcus glycinophilus. II. Enzymes of the acetategenerating system.

Klein, Sigrid M. (Brigham Young University, Provo, Utah) and Richard D. Sagers. Intermediary metabolism of Diplococcus glycinophilus. II. Enzymes of the acetate-generating system. J. Bacteriol. 83:121-126. 1962-The enzymatic steps in the conversion of glycine to acetate by Diplococcus glycinophilus were examined and the reaction rates of the individual steps compared with the maximal glycine fermentation rate by whole cells. Glycine is oxidatively cleaved to one-carbon units with the alpha carbon being transferred to tetrahydrofolate at the oxidation level of formaldehyde. The activated one-carbon unit is condensed with a second glycine molecule to form serine which is then deaminated to pyruvate. Pyruvate gives rise to acetyl units as acetyl coenzyme A and acetyl phosphate. The latter compound reacts with adenosine diphosphate to yield acetate and adenosine triphosphate, providing the main energy-yielding reaction in the fermentation. The enzyme systems discussed together with their specific activities (mumoles substrate acted upon per hr per mg protein) are as follows: serine aldolase, 9 to 12; serine dehydrase, 180; pyruvate-oxidizing and acyl unit-generating system, 96; phosphotransacetylase, 96; acetokinase, 3,600. The high activity of the acetokinase system may tend to pull the entire reaction series in the direction of acetate and adenosine triphosphate generation. In all cases the reaction rates of the individual enzyme systems were equal to or significantly greater than the over-all glycine fermentation rate by whole cells (9 mumoles per hr per mg protein). If coupled together, these enzymes could account for the fermentation of glycine to acetate, CO(2), and ammonia and could account for the conversion of 2-labeled glycine to doubly-labeled acetate as demonstrated in previous tracer studies.

Acetates↗

PubMed1965

Immunological paralysis against type 8 and immunity against type 3 Diplococcus pneumoniae induced by the soluble specific substance of type 8.

Brooke, Marcus S. (Massachusetts Institute of Technology, Cambridge). Immunological paralysis against type VIII and immunity against type III Diplococcus pneumoniae induced by the soluble specific substance of type VIII. J. Bacteriol. 90:1296-1303. 1965.-Mice injected with relatively large quantities of the soluble specific substance of type VIII Diplococcus pneumoniae (SVIII) are, on the basis of challenge experiments, paralyzed against type VIII but immune against type III D. pneumoniae. Their sera contain antibodies which react with sheep cells coated with SIII. Unfortunately, it was not possible to develop an in vitro test with SVIII. When the SVIII was treated with a specific SVIII depolymerase before injection into mice, the sera still contained antibodies against SIII and some protection was afforded these mice against type III but not against type VIII challenge. When the SVIII was treated with a specific SIII depolymerase, antibodies were not detectable and the mice were not protected against type III or type VIII challenge. On the basis of these results it is suggested that either the SVIII strain is a hybrid forming both SVIII and SIII molecules or that part of the SVIII chain is altered to consist of repeating units of cellobiuronic acid rather than alternating units of cellobiuronic acid and the disaccharide galactose-glucose. The quantity of SIII in some preparations of SVIII is calculated to be of the order of 0.01%. It is not clear whether all type VIII strains at all times possess the capacity to elicit antibodies which react specifically against SIII, or if this is the property of only some strains and some preparations of these strains.

Animals↗

PubMed1966

Neuraminidase activity in Diplococcus pneumoniae.

Kelly, R. T. (Marquette University School of Medicine, Milwaukee, Wis.), D. Greiff, and S. Farmer. Neuraminidase activity in Diplococcus pneumoniae. J. Bacteriol. 91:601-603. 1966.-A method for the quantitation of neuraminidase in the presence of N-acetylneuraminic acid aldolase is described. The neuraminidase content of Diplococcus pneumoniae was found to be dependent on the media employed for growth; the highest enzyme activity per milligram of bacterial protein was obtained with Todd-Hewitt broth. Neuraminidase production was stimulated in D. pneumoniae by the addition of N-acetylneuraminlactose, N-acetylneuraminic acid, or N-acetylmannosamine to the growth medium. Three rough strains of D. pneumoniae, which were nonpathogenic for mice, lacked neuraminidase activity. Seven of 12 smooth strains contained neuraminidase; enzyme activity was not detected in the remaining 5 smooth strains. There was no correlation between the presence of neuraminidase activity and the capsular type or between neuraminidase production and animal virulence.

Amines↗

PubMed1966

Bacteriocins of Diplococcus pneumoniae. I. Antagonistic relationships and genetic transformations.

Mindich, Leonard (The Public Health Research Institute of the City of New York, Inc., New York, N.Y.). Bacteriocins of Diplococcus pneumoniae. I. Antagonistic relationships and genetic transformations. J. Bacteriol. 92:1090-1098. 1966.-Several strains of Diplococcus pneumoniae produced bacteriocins inhibiting the growth of other strains of pneumococcus but inactive upon themselves. Strain R6, which did not produce pneumocin under most conditions, was changed to a producing state by mutation or by transformation with deoxyribonucleic acid from other pneumococci. The genetic determinants of several different bacteriocins were introduced into the same cell, where they acted independently. Determinants active in bacteriocin production were also constructed by crosses involving two nonproducing parents. Resistance to pneumocin B4 was a property of cells of the P4 type which produced it. On selection of pneumocin-resistant cells resulting from mutation or transformation in strain R6, resistant cells, all of which were pneumocin producers, were obtained. The genetic determinants of B4 production and resistance were transferred together in transformation. A gene for high level B4 resistance was found in strain P7S. This gene was not associated with B4 production and did not induce production when introduced into R6, although it did increase resistance to B4. Pneumocin B4 was bactericidal and caused a rapid cessation of growth. Its action was inhibited by pronase, trypsin, chymotrypsin, and phospholipids.

Anti-Bacterial Agents↗

PubMed1976

Susceptibility of Staphylococcus aureus, Streptococcus pyogenes and Diplococcus pneumoniae to antibiotics. Comparison of patterns in Poland and Federal Republic of Germany.

One hundred and eighty five strains of Gram-positive cocci were tested for susceptibility to 16 antibiotics, including some newer drugs, by agar dilution technique. Of these, 100 strains (50 each isolated in Poland and Germany) were Staphylococcus aureus, 55 Streptococcus pyogenes, and 30 Diplococcus pneumoniae. Previous investigations of streptococci and pneumococci isolated in Poland and Federal Republic of Grmany, revealed no differences in antibiotic-susceptibility patterns in both countries, which was not the case with staphylococci. Present study demonstrates further evidence for existence of differences in antibiotic-sensitivity of staphylococci, depending of their geographical origin, and presents actual state of susceptibility to antibiotics of Streptococcus pyogenes and Diplococcus pneumoniae.

Anti-Bacterial Agents↗

PubMed1964

THE FINE STRUCTURE OF DIPLOCOCCUS PNEUMONIAE.

The fine structure of an unencapsulated strain of Diplococcus pneumoniae is described. A striking feature of these bacteria is an intracytoplasmic membrane system which appears to be an extension of septa of dividing bacteria. The possible function of these structures and their relationship to the plasma membrane and other types of intracytoplasmic membranes found in pneumococcus is discussed.

Bacteria↗

PubMed1962

Population changes in Diplococcus pneumoniae.

Carta, G. (Wesleyan University, Middletown, Conn.) and W. Firshein. Population changes in Diplococcus pneumoniae. J. Bacteriol. 84:473-477. 1962.-Avirulent mutant strains derived from pneumococcal types I, II, III, and VII established themselves in initially virulent or predominantly virulent populations within 36 to 48 hr of incubation at 37 C in Brain Heart Infusion-blood broth. Aged blood-broth cultures or broth cultures lacking blood permitted a more rapid establishment of avirulent cells. This selective population change was due to a greater viability of avirulent than virulent cells, in the stationary phase, and to a toxic factor, produced by large numbers of avirulent cells, which inhibited the multiplication of virulent cells. Virulent cultures were stabilized, however, by the addition of mixtures of deoxynucleosides and deoxynucleotides, which prevented the establishment of avirulent cells.

Culture Media↗

PubMed1975

Thymidylate synthetase from Diplococcus pneumoniae, properties and inhibition by folate analogs.

Thymidilate synthetase (methylenetetrahydrofolate:dUMP C-methyltransferase) in crude extract from Diplococcus pneumoniae exhibits a partial but variable requirement for Mg-2+ depending upon the buffer. Optimum Mg-2+ concentration is between 0.014 and 0.02 M. The optimum pH for activity in a variety of buffers occurred as a broad peak between 7.0 and 7.7. In Tris/acetate buffer, but not in potassium phosphate buffer, the pH optimum was different in the presence and absence of Mg-2+. Methylation of uridylate, cytidylate and deoxycytidylate could not be demonstrated over a pH range of 5.0-8.0. The enzyme exhibited an apparent Km for deoxyuridylate of 3.08 - 10-5 M and an apparent Km for L-(+)(minus)-5,10-methylene tetrahydrofolate of 2.66 - 10-4 M. During molecular-sieve chromatography and sucrose density-gradient centrifugation, the enzyme was detectable only as a single catalytically active form of Mr 34 000-38 000. 2,4-Diamino quinazoline antifolates were better competitive inhibitors (Ki = 3-8 -10-6 M) of thymidylate synthetase than 2,4-diamino pteridines (Ki = 3- 10-5 M). 2-Amino-4-hydroxy-quinazolines were the best inhibitors (Ki = 1.3-2.9 - 10-6 M). All of the 2,4-diamino quinazolines and pteridines inhibited dihydrofolate reductase from D. pneumoniae in a nearly stoichiometric fashion (Ki = less than 10-10 M). The 2-amino-4-hydroxy-quinazolines were poor inhibitors of this enzyme (Ki = 10=5 M).

Chromatography, Gel↗

PubMed1990

Action of endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. on amino acid-O-glycans: comparison with the enzyme from Diplococcus pneumoniae.

Endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. released the disaccharide, Gal beta 1----3GalNAc, from both dansylated serine-GalNAc-Gal and threonine-GalNAc-Gal, and showed higher activity on the former than the latter. The Km values were 0.17 mM and 1.43 mM with DNS-Ser-GalNAc-Gal and DNS-Thr-GalNAc-Gal, respectively. The optimum pHs were found to be 4.5-7.5 and 4.5-6.0 on DNS-Ser-GalNAc-Gal and DNS-Thr-GalNAc-Gal, respectively. On the contrary, the enzyme from Diplococcus pneumoniae had low activity to release the disaccharide from the amino acid-O-glycans. The possibility that the same O-glycoside but linked to different aglycon amino acids may play a different biological role in glycoproteins is discussed.

Alcaligenes↗

PubMed1985

Isolation and characterization of a new endo-beta-galactosidase from Diplococcus pneumoniae.

An endo-beta-galactosidase, which hydrolyzes the internal beta-galactosidic linkages of R----GlcNAc (or GalNAc) beta 1----3Gal beta 1----4GlcNAc (or Glc), was isolated from the culture supernatant of Diplococcus pneumoniae. The enzyme, named endo-beta-galactosidase DII, hydrolyzed linear N-acetyllactosamine repeating structures in glycolipids and glycopeptides to release oligosaccharides. The specificity of endo-beta-galactosidase DII is the same as that of Escherichia freundii endo-beta-galactosidase as far as described above, but the following differences between these two enzymes were found: Branched lactosaminyl glycolipids and H-antigenic glycolipids were resistant to endo-beta-galactosidase DII, even when linear structure was present at the inner part. Throughout the enzymic hydrolysis, endo-beta-galactosidase DII released mostly small oligosaccharides (tetra-, tri-, and disaccharides) from substrates, suggesting that the enzyme split off the oligosaccharides stepwise from the nonreducing terminal. Lactosaminoglycans were partially hydrolyzed by endo-beta-galactosidase DII to produce small oligosaccharides as the major product and residual glycopeptides. The residual glycopeptides were readily hydrolyzed by E. freundii endo-beta-galactosidase to produce various sizes of oligosaccharides. Keratan sulfate was not degraded by endo-beta-galactosidase DII. These properties of endo-beta-galactosidase DII characterize it as a new endo-beta-galactosidase with a unique specificity.

Anion Exchange Protein 1, Erythrocyte↗

PubMed1997

The substrate specificity of the enzyme endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus pneumonia.

The substrate specificity of the enzyme endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus pneumonia was re-examined using bovine submaxillary mucin and remodelled antifreeze glycoprotein as substrates. Incubation with desialylated bovine submaxillary mucin, which contains six O-linked core types, indicated that the disaccharide Gal beta1-3GalNAc, which is present in very small amount, was the only glycan released, while the disaccharide GlcNAc beta1-3GalNAc, which is the major structure present, and other disaccharides, were not released. To test whether the core disaccharide Gal beta1-3GalNAc with sialic acid linked alpha2-3 to the Gal or linked alpha2-6 to the GalNAc was released, the enzyme was incubated with remodelled antifreeze glycoprotein containing (1) [3H]NeuAc alpha2-3Gal beta1-3GalNAc and (2) Gal beta1-3[[14C]NeuAc alpha2-6]GalNAc as substrates. No NeuAc-containing trisaccharide was released. These results serve to clarify the doubts of many researchers regarding the activity of this enzyme on some newly-described core types and on sialylated substrates.

Animals↗

PubMed1973

Effects of infection with Diplococcus pneumoniae on synthesis of ribonucleic acids in rat liver.

Rats infected with virulent Diplococcus pneumoniae developed a significant increase in the rate of incorporation of labelled orotate into hepatic RNA when compared with pair-fed controls inoculated with heat-killed organisms. The finding was readily detected in rats raised on either a low-protein diet (6% casein) or a diet containing adequate amounts of protein (18% casein). The increase in hepatic RNA synthesis was observed by 12h and was maximal by 16-20h after inoculation with the D. pneumoniae. Most of the infection-related increase in RNA synthesis was associated with the bound ribosomal RNA fraction of the liver. A small but less significant increase was observed in the synthesis of free ribosomal RNA. The increased synthesis of RNA in the liver of infected rats resulted in a marked elevation of the liver RNA/DNA ratio, the major increase being observed in concentration of bound ribosomal RNA fraction. When followed sequentially, the infection-related increase in synthesis of hepatic RNA was preceded by a flux of amino acids into liver and was followed by elevated synthesis rates of serum globulin proteins. These findings suggest that the infectious process was able to regulate hepatic RNA synthesis by altering the rate of transcription of new RNA. This mechanism was stimulated even in rats that had been severely depleted of body protein and amino acids by feeding them on a low-protein diet. The infection-related stimulation of liver RNA and protein synthesis thus appeared to take place at the expense of other body proteins.

Animals↗

PubMed1974

The action of nitrous acid on C-teichoic acid (C-substance) from the walls of Diplococcus pneumoniae.

1. C-teichoic acid (C-substance) from the walls of Diplococcus pneumoniae contained free amino groups accessible to attack by nitrous acid. Treatment with nitrous acid, followed by reduction with borohydride and hydrolysis with acid, gave ribitol, glucitol and their respective phosphates. 2. Hydrolysis of the polymer with alkali followed by treatment of products with nitrous acid yielded glucose. 3. When alkali hydrolysis was followed by treatment with a phosphomonoesterase, nitrous acid degradation of C-substance yielded glucose and a disaccharide identified as 2-O-(N-acetylgalactosaminyl)-d-ribitol. 4. A partial structure for C-teichoic acid was deduced in which the order of the constituent residues and the position of phosphodiester linkages were established.

Borohydrides↗

PubMed1974

Role of a deoxyribonuclease in the genetic transformation of Diplococcus pneumoniae.

Two steps in the uptake of DNA by Diplococcus pneumoniae were characterized by analyzing mutants defective in transformation. A strain deficient in the two major deoxyribonucleases of D. pneumoniae takes up DNA normally and converts it to single strands within the cell and oligonucleotide fragments outside the cell. Extracts of this strain contain a residual deoxyribonuclease that produces similar oligonucleotide fragments in vitro. This enzyme is missing in transformation-defective mutants blocked in the second or entry step. Cells of this mutant class bind large amounts of DNA to their surface in a form accessible to external agents. Another class of nontransformable mutants fails to bind DNA at all. Their deoxyribonuclease content is unchanged, and they are apparently blocked in the first or binding step of DNA uptake. The binding step requires a source of energy and prior activation of the cells by competence factor. Entry may be independent of these requirements and may come about by action of the deoxyribonuclease on one strand of DNA with energy for the transport of the intact strand deriving from hydrolysis of the degraded strand. The enzyme may thus act as a DNA translocase.

Binding Sites↗

PubMed1973

Hyperproduction of dihydrofolate reductase in Diplococcus pneumoniae after mutation in the structural gene. Evidence for an effect at the level of transcription.

Dihydrofolate reductase is markedly hyperproduced in strains of Diplococcus pneumoniae which bear any one of a unique group of sense to sense mutations (ame(r)) in the corresponding structural gene. Increased enzyme levels mediated by the ame(r) mutations are apparently the result of increased rates of de novo synthesis. The basis for these effects could be transcriptional, translational or could involve an increase in messenger RNA stability. Data revealing no difference in stability of the related mRNA in a variety of mutants and the wild-type strain appear to eliminate the last possibility. Other data support the idea of an effect on transcription. This includes the extreme sensitivity of ame(r) mutation expression following genetic transformation, to inhibition by actinomycin D and rifampacin, and the presence in one extremely high level mutant (ame(r)-3 with 120 times the wild-type enzyme content) of increased amounts of mRNA. The data are most compatible with the idea of a regulatory function for the dihydrofolate reductase protein in this organism.

Carbon Isotopes↗

PubMed1976

Partial purification and characterization of an endo-alpha-N-acetylgalactosaminidase from the culture of medium of Diplococcus pneumoniae.

The culture medium of Diplococcus pneumoniae contains enzymic activity that cleaves Galbeta1 leads to 3GalNAc from desialized human erythrocyte membrane glycoprotein. The enzyme was purified 180-fold by ammonium sulfate fractionation, gel filtration through a Sephadex G-200 column, and DEAE A-25 Sephadex chromatography. The purified enzyme liberates Galbeta1 leads to 3GalNAc from glycopeptides and glycoproteins with Galbeta1 leads to 3GalNAcalpha1 leads to Ser and Thr moieties. The optimum pH of this enzyme is 6.0. Using glycopeptides obtained by trypsin digestion of human erythrocyte membrane glycoprotein as a substrate, a Km of 0.20 mM (on the basis of the amount of Galbeta1 leads to 3GalNAc residues) was obtained. So far, the enzyme appears to have a strict specificity for Galbeta1 leads to 3GalNAcalpha1 leads to Ser and Thr structures, because no oligosaccharides larger than trisaccharides were liberated from porcine submaxillary mucin.

Cations, Divalent↗