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T S Theodore

Publications and source records attributed to T S Theodore.

At least 37 records · Page 2Linked to original sources
PubMed1981

Streptolysin S activation by lipoteichoic acid.

Lipoteichoic acid from streptococci and Staphylococcus aureus both activated membrane-bound precursor streptolysin S and induced the formation of extracellular streptolysin S. Lipoteichoic acid could replace other substances, such as yeast ribonucleic acid core, that act as carriers for hemolysin but which are not components of the streptococcus or the host. Lipoteichoic acid may play a role as the physiological carrier of streptolysin S to host tissues.

Bacterial Proteins↗
PubMed1979

Polypeptides of simian rotavirus (SA-11) determined by a continuous polyacrylamide gel electrophoresis method.

Simian rotavirus (SA-11) isolated from infected African green monkey kidney cells was separated into two virus fractions in a CsCl density gradient and their proteins analysed on a continuous phosphte buffered polyacrylamide gel electrophoresis system. One peak (buoyant density 1.37 g/ml) contained double capsid virus particles which were radioimmunoassay (RIA)- and haemagglutinin (HA)- positive and yielded eight polypeptides whose mol. wt. ranged from 48,000 to 128,000. The second peak (buoyant density 1.39 g/ml) which contained 70% single capsid particles and was RIA-positive but HA-negative, yielded only five polypeptides. The three polypeptides missing in the second peak are associated presumably with the outer capsid of SA-11 virus particles and one or more of these is assumed to be the HA of SA-11 rotavirus.

Animals↗
PubMed1978

Biochemical differences between serotypes of Cryptococcus neoformans.

Prior studies have shown that C. neoformans isolates belonging to serotypes B and C differed from serotype A and D isolates in respect to the morphology of the perfect state, geographic distribution within the U.S.A. and frequency of isolation from avian droppings. The current study found that uptake of radiolabeled l-malic acid was approximately tenfold greater in serotype B and C than in A and D isolates. Assimilation of l-malic, fumaric and succinic acids also distinguished serotypes B and C from A and D. Greening of Guizotia seed agar occurred with 18 of 32 serotype B and C but in none of 91 serotype A or D isolates. The one property not following the same line of division was relatively slow creatinine assimilation, which distinguished type A alone.

Creatinine↗
PubMed1975

Cellular location of alpha-hemolysin in Staphylococcus aureus.

Protoplast fractionation techniques were used to prepare subcellular fractions of three strains of Staphylococcus aureus for the analysis of alpha-hemolysin activity. More than 90% of the cellular hemolytic activity was localized in the periplasm, only a trace was detected in the cytoplasm, and none was found in either plasma membranes or mesosomes. This cellular portion constituted approximately 4 to 10% of the total hemolytic activity of the culture. The erythrocyte lysis spectrum and Sephadex G-100 filtration studies indicated that the cellular hemolysin closely resembles the extracellular form.

Animals↗
PubMed1975

Cellular location of streptolysin O.

Streptolysin O was measured in subcellular fractions of group A streptococci obtained after preparation of protoplasts in a hypertonic buffer containing raffinose. Most of the activity was located in the periplasm (the region between cell wall and membrane) and did not differ in several characteristics from that of extracellular streptolysin O. Of the enzymes used as subcellular markers, aldolase and maltase (cytoplasmic) and acid phosphatase (membrane associated) were in the same fractions as found in other bacteria. However, the location of alkaline phosphatase differed from that of other bacteria in the most of the activity was in cytoplasm rather than in the periplasm.

Cytoplasm↗
PubMed1975

Characterization of the lipids of mesosomal vesicles and plasma membranes from Staphylococcus aureus.

Mesosomal vesicles and plasma membranes were isolated from Staphylococcus aureus ATCC 6538P by protoplasting and differential centrifugation. The lipids of each of the two membrane fractions were extracted with pyridine-acetic acid-N-butanol, and the nonlipid contaminants were removed by Sephadex treatment. The lipids were then separated by passage through diethylaminoethyl-cellulose columns and characterized by thin-layer chromatographic, chemical, and spectral analyses. The lipids were separated into four discrete diethylaminoethyl fractions: (i) vitamin K2, carotenoids, C55 isoprenoid alcohol, and monoglucosyl diglyceride; (ii) cardiolipin, carotenoids, phosphatidyl glycerol, diglucosyl diglyceride, and an unidentified ninhydrin-positive component; (iii) cardiolipid and phosphatidyl glyderol; (iv) cardiolipin, phosphatidyl glycerol, and phosphatidyl glucose. Qualitatively, no difference in lipid composition between mesosomal vesicles and plasma membranes was found. However, based on equal dry weights of membrane materials, a relative quantitative difference in the amount of specific lipids in mesosomal vesicles and plasma membranes was observed. There are 4 times more monoglucosyl diglyceride, 2.6 times more diglucosyl diglyceride, 3.8 times more phosphatidyl glucose, 2 times more carotenoids, and 2 times more vitamin K2 found in mesosomal vesicles than in plasma membranes. The concentration of cardiolipin and phosphatidyl glycerol is 3.6 and 6 times greater, respectively, in mesosomal vesicles.

Cardiolipins↗
PubMed1974

Lipoteichoic acid localization in mesosomal vesicles of Staphylococcus aureus.

Mesosomal vesicles and plasma membranes of Staphylococcus aureus ATCC 6538P have been prepared and examined for the presence of lipoteichoic acid. Lipids were first removed by treatment with pyridine-acetic acid-butanol (22:31:100, vol/vol/vol) and chloroform-methanol (2:1, vol/vol). Subsequently, lipoteichoic acid was removed with 40% phenol in water. The lipoteichoic acid from mesosomal vesicles was characterized by (i) equimolar glycerol and phosphate, (ii) alanine upon hydrolysis (2 N NH(4)OH, 18 h, 22 C), and (iii) fatty acids, diglycerol triphosphate, glycerol monophosphate, and glycerol diphosphate upon alkaline hydrolysis (1 N NaOH, 3h, 100 C). The plasma membranes contained no lipoteichoic acid. The presence in mesosomal vesicles of 18% of the dry weight as lipoteichoic acid and its absence from plasma membranes provide the first major chemical differences between these organelles. A study of the lipoteichoic acid content in various fractions of the cell showed that the mesosomal vesicles were the major and probably the sole site for the localization of the lipoteichoic acid in these organisms. A new method for the preparation of mesosomes in increased yields is reported. A theory for the control of cell division involving lipoteichoic acid and the mesosome is proposed.

Cell Fractionation↗
PubMed1974

Cellular location of degradative enzymes in Staphylococcus aureus.

Staphylococus aureus, ATCC 6538P, was fractionated into protoplast membranes, mesosomal vesicles, periplasm, and cytoplasm. These fractions and the culture fluid were then assayed for various degradative enzyme activities. They were not restricted to a single fraction nor dispersed homogeneously, but were distributed predominantly (on the basis of specific activity) as follows: nuclease in the culture fluid; alkaline phosphatase, 5'-nucleotidase, and acid phosphatase in the periplasm; adenosine triphosphatase in the protoplast membrane; and protease (low levels) in mesosomal vesicles. No significant esterase nor cell wall hydrolytic activity was found in any fraction. S. aureus 80/81 was studied for penicillinase activity after induction with benzyl penicillin; this enzyme was localized in the mesosomal vesicles. Electron microscopy did not reveal any ultrastructural changes associated with secretion of the extracellular fraction. Overall, these studies demonstrate that degradative enzymes are located in several surface compartments and that, therefore, the mesosome does not function as a prototype lysosome in S. aureus.

Acid Phosphatase↗
PubMed1973

Protein and fatty acid composition of mesosomal vesicles and plasma membranes of Staphylococcus aureus.

Qualitatively, the protein and fatty acid composition of purified mesosomal vesicles and the plasma membrane isolated from Staphylococcus aureus ATCC 6538P are identical, the major difference between these two cellular components being only quantitative in nature. Mesosomal vesicles and plasma membranes, when subjected to acidic or neutral disk gel electrophoresis, exhibited more than 22 bands of protein. With urea-acetic acid gels, the plasma membrane had a higher concentration of "slower-migrating proteins" whereas "faster-migrating proteins" predominated in the mesosomal vesicles. With neutral disk gel electrophoresis, mesosomal vesicles exhibited one prominent protein band with an approximate molecular weight of 35,000 and which was four times greater than that found in the corresponding region on gels of the plasma membrane. Finally, fatty acid analyses by capillary column gas chromatography showed that although the fatty acid composition is the same, the fatty acid content in mesosomal vesicles is 48% greater than that of the plasma membrane. The dominant fatty acids in both of these cellular components are the iso and anteiso branched methyl C15, C17, and C19 fatty acids and comprise at least 85% of the total fatty acids extracted. These results show that distinct chemical differences exist between the mesosomal vesicles and the plasma membrane of Staphylococcus aureus.

Bacterial Proteins↗
PubMed1971

Polyacrylamide gel identification of bacterial L-forms and Mycoplasma species of human origin.

Polyacrylamide gel electrophoretic patterns of acidified phenol extracts prepared from whole cells can be used for the identification of bacterial L-forms and Mycoplasma species of human origin. Ten human Mycoplasma serotypes and eight L-forms belonging to five different genera were studied. The gel patterns were sufficiently distinct and reproducible that it was possible not only to identify L-forms at the genus level (group with streptococci) and different Mycoplasma serotypes but also to differentiate between the two of them. The parentage of L-forms of Streptobacillus moniliformis L1, Listeria monocytogenes, Streptococcus MG, and Staphylococcus aureus Smith strain was established by relating their gel patterns directly to parent bacteria. It was found that an L-form designated S. moniliformis An (ATCC 14220) was actually an L-form of Proteus. In addition, it was shown electrophoretically that no relationship existed between the Streptococcus MG L-form and M. pneumoniae. The applicability of this method as a diagnostic and taxonomic tool for the differentiation of L-forms and mycoplasmas is discussed.

Acrylates↗
PubMed1971

Electron microscopy during release and purification of mesosomal vesicles and protoplast membranes from Staphylococcus aureus.

The mesosomes of log-phase Staphylococcus aureus ATCC 6538P and Staphylococcus aureus phage-type 80/81, as seen in situ in ultrathin sections, were of the vesicular type. The constituent vesicles ranged from 35 to 50 nm in diameter when the glutaraldehyde-osmium-uranium-lead sequence of fixation and staining was used. During protoplasting in hypertonic buffer containing a muralytic enzyme, vesicles of the same size were extruded and required magnesium ion to maintain structural integrity. The vesicles, purified from the protoplasting supernatant medium by density gradient centrifugation, maintained size and configuration in a homogeneous preparation. Cytoplasmic membranes, produced by osmotic shock and nuclease treatment of protoplasts, were similarly concentrated in gradients. However, they were not free of membrane-associated ribosomes nor of mesosomal vesicles except when prepared in the absence of magnesium.

Acetates↗
PubMed1970

Protein difference between competent and noncompetent cultures of a group H Streptococcus.

Acidified phenol extracts prepared from competent cultures of a group H Streptococcus strain Wicky made competent with competence factor derived from cultures of another group H Streptococcus, strain Challis, showed a difference in polyacrylamide-gel protein patterns when compared to extracts prepared from noncompetent cultures of strain Wicky. The prominent single protein band difference did not appear when Wicky cells were simultaneously treated with competence factor and chloramphenicol, an inhibitor of the development of competence. Chloramphenicol had no effect on transformation nor the appearance of the "new" protein band when added to fully competent cells. This new protein, which is associated with the appearance of competence, seems to be synthesized as a result of induction by competence factor; its exact role, however, is as yet unknown.

Bacterial Proteins↗
PubMed1969

Generic identification of L-forms by polyacrylamide gel electrophoretic comparison of extracts from parent strains and their derived L-forms.

A polyacrylamide gel electrophoretic method was used for identification of L-forms in the genera Streptococcus, Staphylococcus, and Proteus, by comparing phenol-acetic acid-water extracts of homologous parent L-form pairs to one another and to other pairs. The method requires only milligram quantities of material for analysis. The standard patterns for the strains used in this study are shown as pictures of the gels and as densitometric tracings of appropriate gels. They show that, despite occasional minor differences in some organisms, the gel electrophoretic patterns of homologous L-forms and bacterial pairs are sufficiently similar-as well as sufficiently dissimilar from patterns of other genera-to permit generic identification of an unknown L-form by reference to patterns derived from possible parental bacteria.

Acrylates↗
PubMed1969

Identification of L forms by polyacrylamide-gel electrophoresis.

Crude membranes were obtained from L forms by allowing the cells to lyse in distilled water. The crude membranes were washed several times in distilled water, lyophilized, and extracted with phenol-acetic acid-water. The membrane proteins were separated electrophoretically in polyacrylamide gels run at pH 4.5. Electrophoretic patterns and densitometric tracings of the gels showed distinct, reproducible intergeneric differences among L forms of Proteus, Streptobacillus, Staphylococcus, and Streptococcus. Differences within a genus could not be detected except between the group A streptococcal L forms and the one group D F-24 L form. This electrophoretic method offers possibilities for ready identification of L forms through the use of standard reference strains.

Bacterial Proteins↗