scholarly journals STUDIES ON THE CHEMISTRY AND IMMUNOCHEMISTRY OF CELL WALLS OF STAPHYLOCOCCUS AUREUS

1962 ◽  
Vol 116 (2) ◽  
pp. 229-245 ◽  
Author(s):  
Stephen I. Morse
Keyword(s):  
Staphylococcus Aureus ◽  
Glutamic Acid ◽  
Cell Walls ◽  
Antigenic Determinant ◽  
Intact Cell ◽  
Teichoic Acid ◽  
The Other ◽  
Aureus Strain ◽  
Muramic Acid ◽  
Sheep Erythrocytes

The cell walls of an 80/81 strain of Staphylococcus aureus (NYH-6) contain alanine, glycine, glutamic acid, lysine, muramic acid, glucosamine, and ribitol phosphate. 94 per cent of the phosphorus and 41 per cent of the glucosamine are removed by extraction of the cell walls with hot 5 per cent TCA, but significant amounts of the other constituents are not extracted by this procedure. The residue after hot TCA extraction (mucopeptide) is susceptible to lysozyme whereas the intact cell walls are resistant. Staphylococcus aureus cell walls are agglutinated by S. aureus antisera. Agglutination of the cell walls of one S. aureus strain is inhibited by absorption of antisera with cell walls of other S. aureus strains but not by absorption with S. albus cell walls. The ribitol teichoic acid can be isolated from cold TCA extracts of the cell walls. This compound consists almost entirely of ribitol phosphate and glucosamine. The isolated teichoic acid of strain NYH-6 is readily fixed to tanned sheep erythrocytes and these sensitized cells are agglutinated by S. aureus antisera. Cold TCA extracts of cell walls of other strains of S. aureus inhibit hemagglutination whereas extracts of S. albus walls do not. Studies on the inhibition of both hemagglutination and precipitation indicate that the antigenic determinant of S. aureus NYH-6 teichoic acid is ß-N-acetylglucosamine.

Die Aminosäuresequenz des Ornithin und Lysin enthaltenden Mureins einiger Stämme von Lactobacillus bifidus aus dem Pansen /The amino acid sequence of the ornithine and lysine containing mureins of some strains of Lactobacillus bifidus isolated from rumen

1969 ◽  
Vol 24 (12) ◽  
pp. 1524-1528 ◽  
Author(s):  
Wilhelm Holzapfel ◽  
Vittoria Scardovi ◽  
Otto Kandler
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glutamic Acid ◽  
Cell Walls ◽  
Teichoic Acid ◽  
The Other ◽  
Molar Ratio ◽  
Partial Hydrolysis ◽  
Muramic Acid ◽  
Diamino Acid

Cell walls of six strains of Lactobacillus bifidus (recently classified as Bifidobacterium globosum) isolated from the rumen of sheep were isolated by lysing the cells with glass beads followed by tryptic digestion. No teichoic acid could be found. The polysaccharide consists of galactose, rhamnose and glucosamine. The murein (peptidoglycan) contains MurNAc, GlcNH2NAc, Glu, Ala, and diamino acids in a molar ratio of 1:1:1:5:1. Both diamino acids, lysine and ornithine are present. In two strains they occur in about equal amounts, while in the other four strains ornithine is predominant. The lysis of the cell walls by lysozyme resulted in a mixture of two types of muropeptides: One contains lysine, the other ornithine.The amino acid sequence was determined by analysing the oligopeptides arising during acid partial hydrolysis. It was shown, that the tetrapeptides attached to the muramic acid are equal to those of other mureins: L-Ala-γ-D-Glu-L-Lys (L-Orn) -D-Ala. Glutamic acid is probably amidated, since the total hydrolysate contained slightly more than one mole of NH3 per mole of glutamic acid. The cross-liking peptide is a tri-alanine, which is bound to the ω-aminogroup of the diamino acid of one tetrapeptid and to the C-terminal D-alanine of another. Since about 2 —4% of the alanine is N-terminal in the cell wall, 10 to 20% of the interpeptide bridges are probably not cross linked. In addition 2 — 3% of the diamino acids are ω-N-terminal and therefore not substituted by a trialanine. A small percentage of D-alanine and of the diamino acids is C-terminal. The latter indicates, that some of the peptide subunits are incomplete i.e.. the terminal D-alanine is missing.

scholarly journals CHEMICAL BASIS FOR AN IMMUNOLOGICAL SPECIFICITY OF A STRAIN OF STAPHYLOCOCCUS AUREUS

1963 ◽  
Vol 117 (6) ◽  
pp. 925-935 ◽  
Author(s):  
William G. Juergens ◽  
Arnold R. Sanderson ◽  
Jack L. Strominger
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Degradation Product ◽  
Cell Walls ◽  
Horse Serum ◽  
Teichoic Acid ◽  
Aureus Strain ◽  
Chemical Basis ◽  
Immunological Specificity ◽  
Group A

Antisera, prepared against formalin-killed cells of Staphylococcus aureus, strain Copenhagen, agglutinated the cell walls of this strain. The agglutination was inhibited by the teichoic acid from the cell wall of this strain, by any degradation product of this teichoic acid which contained the α-acetylglucosaminyl-ribitol unit, by α-phenyl-acetylglucosaminide, and by N-acetylglucosamine, but not by a large number of other haptens related to the cell wall. In quantitative experiments, however, only 40 to 50 per cent of antibody adsorption to cell wall could be inhibited by teichoic acid or by N-acetylglucosamine. The α-acetylglucosaminyl-ribitol unit in the teichoic acid is, therefore, an important immunological determinant in the cell wall of this strain, although other immunological specificities may also exist. The cell walls were also agglutinated by heterologous antisera prepared against streptococcal Group A carbohydrate or against horse serum azophenyl-ß-acetylglucosaminide. The heterologous agglutination, however, was specific for the ß-acetylglucosaminyl-ribitol units in the teichoic acid.

scholarly journals Die Aminosäuresequenz des Serin und Asparaginsäure enthaltenden Mureins von Bifidobacterium bifidum Orla Jensen/ The amino acid sequence of the serin and aspartic acid containing mureins of Bifidobacterium bifidum ORLA JENSEN

1970 ◽  
Vol 25 (11) ◽  
pp. 1294-1301 ◽  
Author(s):  
Dieter Koch ◽  
Karl Heinz Schleifer ◽  
Otto Kandler
Keyword(s):  
Cell Wall ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Cell Walls ◽  
Teichoic Acid ◽  
Bifidobacterium Bifidum ◽  
Muramic Acid ◽  
Partial Acid Hydrolysis

Cell walls of Bifidobacterium bifidum var. pennsylvanicus were isolated. The polysaccharide consisted of glucose, galactose and rhamnose. Teichoic acid was not present. The murein (peptidoglycan) contained MurNAc, GlcNH2NAc, ᴅ-Glu, Ala. ʟ-Ser, ᴅ-Asp and L-Orn in a ratio of about 1 : 1 : 1 : 2 : 1 : 1 : 1. In one batch a high amount of ʟ-glutamic acid was found. It was not a constituent of the murein since it remained in the lysozyme insensitive residue.The amino acid sequence of the murein was determined by analyzing the oligopeptides arising during partial acid hydrolysis. It was shown that the peptide subunits attached to the muramic acid are the same as in many other mureins: ʟ-Ala-ᴅ-Glu-ʟ-Orn-D-Ala. The interpeptide bridge consisted of β-ᴅ-aspartyl-ʟ-serine. Since about 35% of aspartic acid and 6% of ornithine are N-terminal in the cell wall, it was assumed that only 60% of the peptide subunits are cross-linked. 4 other strains of B. bifidum proved to contain the same type of murein. While all other strains of other species of Bifidobacterium investigated contained other types of murein, it seems likely that the Orn-Ser-Asp type of the murein is typical of B. bifidum.

The physiology of teichoic acid deficient staphylococci

1973 ◽  
Vol 19 (11) ◽  
pp. 1393-1399 ◽  
Author(s):  
Li-Tse Ou ◽  
A. N. Chatterjee ◽  
F. E. Young ◽  
R. E. Marquis
Keyword(s):  
Cell Walls ◽  
Parent Strain ◽  
Teichoic Acid ◽  
Low Ph ◽  
Aureus Strain ◽  
Binding Affinities ◽  
Inhibitory Effects ◽  
Growth Inhibitory ◽  
Acid Titration ◽  
Phosphate Groups

Cell walls isolated from a teichoic acid deficient mutant (52A5) of Staphylococcus aureus strain H were found to have lower capacities to bind cations than did walls of the parent strain. Both types of walls had higher binding affinities for Mg2+ and Ca2+ than for K+ and Na+. The reduced number of phosphate groups in 52A5 walls was reflected in a higher apparent pKa of 4.3 for displacement of Mg2+ (or Ca2+) during acid titration with HCl. The comparable pKa value for displacement of bound Mg2+ from parent-strain walls was 3.7. The reduced capacity of 52A5 walls to bind cations was not reflected in any significant increase in sensitivity to the growth inhibitory actions of ethylenediaminetetraacetate, low pH, or high NaCl concentrations. However, the 52A5 strain was somewhat more sensitive to the inhibitory effects of high pH. Also, mutant walls were found to be structurally more compact than walls of the parent strain, presumably because of less extensive electrostatic repulsion within the wall matrix.

scholarly journals The linkage of sugar phosphate polymer to peptidoglycan in walls of Micrococcus sp. 2102

1978 ◽  
Vol 169 (2) ◽  
pp. 329-336 ◽  
Author(s):  
J Heptinstall ◽  
J Coley ◽  
P J Ward ◽  
A R Archibald ◽  
J Baddiley
Keyword(s):  
Staphylococcus Aureus ◽  
Alkaline Hydrolysis ◽  
The Other ◽  
Muramic Acid ◽  
Sugar Phosphate ◽  
Glycerol Phosphate ◽  
Homogeneous Product ◽  
A Chain

1. Protein-free walls of Micrococcus sp. 2102 contain peptidoglycan, poly-(N-acetylglucosamine 1-phosphate) and small amounts of glycerol phosphate. 2. After destruction of the poly-(N-acetylglucosamine 1-phosphate) with periodate, the glycerol phosphate remains attached to the wall, but can be removed by controlled alkaline hydrolysis. The homogeneous product comprises a chain of three glycerol phosphates and an additional phosphate residue. 3. The poly-(N-acetylglucosamine 1-phosphate) is attached through its terminal phosphate to one end of the tri(glycerol phosphate). 4. The other end of the glycerol phosphate trimer is attached through its terminal phosphate to the 3-or 4-position of an N-acetylglucosamine. It is concluded that the sequence of residues in the sugar 1-phosphate polymer-peptidoglycan complex is: (N-acetylglucosamine 1-phosphate)24-(glycerol phosphate)3-N-acetylglucosamine 1-phosphate-muramic acid (in peptidoglycan). Thus in this organism the phosphorylated wall polymer is attached to the peptidoglycan of the wall through a linkage unit comprising a chain of three glycerol phosphate residues and an N-acetylglucosamine 1-phosphate, similar to or identical with the linkage unit in Staphylococcus aureus H.

COMPOSITION OF PURIFIED MUCOPEPTIDE FROM THE WALL OF AEROBACTER CLOACAE

1962 ◽  
Vol 8 (1) ◽  
pp. 89-98 ◽  
Author(s):  
A. J. Schocher ◽  
S. T. Bayley ◽  
R. W. Watson
Keyword(s):  
Glutamic Acid ◽  
Acid Hydrolysis ◽  
Teichoic Acid ◽  
Sodium Lauryl Sulphate ◽  
Diaminopimelic Acid ◽  
Peptide Chain ◽  
Muramic Acid ◽  
Aqueous Sodium ◽  
Molar Ratios ◽  
Saturated Aqueous Sodium

Molecular proportions of glucosamine, muramic acid, alanine, glutamic acid, and diaminopimelic acid in purified mucopeptide (MP) from the wall of Aerobacter cloacae NRC 492 have been estimated. Crude walls, obtained by fractional centrifugation of disintegrated log-phase cells, were treated with trypsin, ribonuclease, and pepsin to remove cytoplasmic contaminants. Of a number of protein solvents tested on the isolated walls, saturated aqueous sodium lauryl sulphate gave the purest MP in the highest yield. Molar ratios of glucosamine, muramic acid, alanine, glutamic acid, and diaminopimelic acid in hydrolyzates of the MP, corrected for the loss of hexosamines under the conditions of acid hydrolysis, were 2:2:3:2:2 respectively. These ratios indicate the presence of two types of peptide, with one peptide chain attached to each disaccharide unit. Analysis showed the absence of phosphate and therefore of teichoic acid from the purified MP.

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