Biomedical subjects

V M Reusch

Publications and source records attributed to V M Reusch.

11 recordsLinked to original sources

PubMed1984

Lipopolymers, isoprenoids, and the assembly of the gram-positive cell wall.

Several lines of evidence suggest that Gram-positive bacterial cell surface polymers are synthesized by stepwise addition of polymer subunits to an amphipathic acceptor. In the case of membrane-bound lipopolymers such as mannan and lipoteichoic acid, the finished product may be covalently linked to a lipid anchor. In the case of polymers that are transferred into preexisting cell wall, such as teichoic acid and peptidoglycan, two alternative fates might be possible: (1) transfer into wall with concomitant or later cleavage of the lipid anchor, with recycling of the lipid anchor or secretion of the lipid anchor into the growth medium, and (2) transfer into wall without cleavage of the lipid anchor, resulting in maintenance of the covalent relationship between lipid anchor and polymer chain. In the latter case, a close relationship should be established between the cell wall and the plasma membrane. A number of Gram-positive bacteria have been shown to be resistant to plasmolysis. Therefore, a model for the assembly of the Gram-positive cell wall is proposed which takes into account a role for lipopolymeric intermediates and which views the establishment of resistance to plasmolysis as the natural consequence of such a mechanism.

Cell Membrane↗

PubMed1983

Specific coaggregation and the cell wall of Streptococcus sanguis.

Sacculi prepared from Streptococcus sanguis 34 by extensive extraction of cells with hot sodium dodecyl sulfate-2-mercaptoethanol retained the ability to coaggregate with Actinomyces viscosus T14V. When S. sanguis 34 was disrupted by homogenization with glass beads and fractionated by differential centrifugation, only the cell wall fraction agglutinated A. viscosus T14V. When strain 34 was treated with lysozyme, the coaggregating capability of the cells was essentially unaltered. Sacculi prepared from lysozyme-treated strain 34 and additionally purified by electrophoresis were agglutinated by strain T14V.

Actinomyces↗

PubMed1982

Isolation and analysis of sacculi from Streptococcus sanguis.

Sacculi were prepared from Streptococcus sanguis 34 by exhaustive extraction of bacteria with hot 1% sodium dodecyl sulfate-0.5% 2-mercaptoethanol. Lyophilized residue was dissociated by brief sonication to single bodies closely resembling streptococci in phase-contrast microscopic density, staining properties, and morphology. Electron micrographs revealed bodies that contained variable amounts of cellular contents and were bounded by intact cell walls. Chemical analyses of sacculi demonstrated the presence of peptidoglycan, carbohydrate, protein, and phosphate. The hexose content of sacculi varied 10-fold depending upon the composition of the growth medium. When sacculi were subjected to treatment with 5 M LiCl, 8 M urea, 40% phenol (25 degrees C), or dimethyl sulfoxide most of the nitrogen and carbohydrate present was recovered in the insoluble fraction. These data suggest that sacculi contain the cell wall fraction of the extracted bacteria and that most of the carbohydrates and proteins of sacculi are firmly bound to the insoluble fraction, which contains the peptidoglycan matrix.

Bacterial Proteins↗

PubMed1982

Levels of cell wall enzymes in endospores and vegetative cells of Bacillus subtilis.

Vegetative bacilli and refractile endospores of Bacillus subtilis 168 were disrupted by homogenization with glass beads and fractionated by differential centrifugation. Most of the protein of endospores was particulate, whereas for bacilli most was soluble. Alanine racemase activity was sixfold higher in extract of endospores than in extract of bacilli and was particulate, whereas the enzyme from bacilli was soluble. The specific activities of seven other enzymes involved in peptidoglycan and teichoic acid biosynthesis were higher in extracts of bacilli than in those of endospores. The results suggest that restoration of activities of these seven enzymes to vegetative levels occurs during germination and outgrowth.

Alanine Racemase↗

PubMed1977

Synthesis of "group polysaccharide" by membranes from Streptococcus pyogenes and its stabilized L-form.

Rhamnose and N-acetylglucosamine (GlcNAc) are incorporated from thymidine 5'-diphosphorhamnose and uridine 5-diphospho-N-acetylglucosamine (UDPGlcNAc) into membrane fragments prepared from Streptococcus pyogenes but not into membrane fragements prepared from a stabilized L-form of this organism. Incorporation from TDPrhamnose is partially dependent upon UDPGlcNAc and vice versa. The oligomeric GlcNAc and rhamonose-containing products are easily extracted from membrane particles by sedimentation through detergent solutions. They are substantially extracted into methanol but not into chloroform-methanol (2:1). When product containing both radioactive rhamnose and GlcNAc is deacetylated and hydrolyzed briefy in acid, glucosaminyl rhamnose is obtained, byt not higher oligomers, suggesting that oligomer synthesis in vitro is terminated because unidentified wnzymatic requirements are not satisfied. The data are consistent with the assembly of group A-specific polysaccharide at the cellular membrane with participation of a lipoid anchor (acceptor) molecule.

Acetylglucosamine↗

PubMed1976

Defective synthesis of lipid intermediates for peptidoglycan formation in a stabilized L-form of Streptococcus pyogenes.

Membrane preparations obtained from a stabilized L-form of Streptococcus pyogenes are incapable of synthesizing peptidoglycan from uridine-5'-diphospho-N-acetyl-D-muramyl-L-Ala-D-iso-Glu-L-Lys-D-Ala-D-Ala and uridine-5'-diphospho-N-acetyl-D-glucosamine, in contrast with similar preparations from the parental streptococcus. Furthermore, 50-fold higher levels of lipid intermediates which serve as membrane-bound substrates for peptidoglycan synthesis are synthesized in reaction mixtures containing streptococcal membranes than with similar preparations from the L-form. These observations suggest that the inability of this stabilized L-form to form a cell wall in vivo lies, at least in part, in its failure to synthesize significant quantities of the lipid substrates for peptidoglycan synthesis.

Adenosine Triphosphate↗

PubMed1974