scholarly journals LOCATION AND COMPOSITION OF SPORE MUCOPEPTIDE IN BACILLUS SPECIES

1963 ◽  
Vol 16 (3) ◽  
pp. 593-609 ◽  
Author(s):  
A. D. Warth ◽  
D. F. Ohye ◽  
W. G. Murrell
Keyword(s):  
Heat Resistance ◽  
Glutamic Acid ◽  
Electron Micrographs ◽  
Bacillus Coagulans ◽  
Diaminopimelic Acid ◽  
Bacillus Species ◽  
Muramic Acid ◽  
Cortical Structure

Spore integuments of Bacillus coagulans were prepared containing nearly all the hexosamine and α, ϵ-diaminopimelic acid (DAP) present in intact spores. Subsequent autolytic action resulted in the destruction and removal of the residual cortical structure and "cortical membrane" leaving the appearance of the inner and outer spore coats unchanged in electron micrographs. Concurrently, all the hexosamine and DAP in the preparation was released mainly as non-diffusible mucopeptide containing alanine, glutamic acid, DAP, and all the glucosamine and muramic acid. Some diffusible peptides containing alanine, glutamic acid, and DAP were also present but there was little protein or carbohydrate. Lysozyme digestion of integument preparations from heated spores of Bacillus 636, B. subtilis, B. coagulans, and B. stearothermophilus specifically removed the residual cortex and cortical membrane with the release of the mucopeptide. In B. cereus T, only the residual cortex and part of the mucopeptide were solubilized by lysozyme. The effect of several reagents and enzymes upon the appearance and removal of hexosamine from B. coagul ans spore integuments is reported. The results show that spore mucopeptide is mainly located in the residual cortex and cortical membrane and suggest that these structures consist essentially of mucopeptide. The implications of these results in relation to the "contractile cortex" theory of heat resistance in spores are discussed.

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.

scholarly journals THE COMPOSITION AND STRUCTURE OF BACTERIAL SPORES

1963 ◽  
Vol 16 (3) ◽  
pp. 579-592 ◽  
Author(s):  
A. D. Warth ◽  
D. F. Ohye ◽  
W. G. Murrell
Keyword(s):  
Electron Microscopy ◽  
Cell Wall ◽  
Heat Resistance ◽  
Dipicolinic Acid ◽  
Diaminopimelic Acid ◽  
Bacterial Spores ◽  
Bacillus Species ◽  
Thin Sections ◽  
Composition And Structure ◽  
Soluble Fractions

The composition of the insoluble "integuments" and soluble "contents" fractions of spores of four Bacillus species of widely differing heat resistance were compared. Electron microscopy of thin sections was also used to determine and compare the morphological structures in the integument preparations. The soluble fractions of the thermophiles, B. coagulans and B. stearothermophilus, had a higher content of hexose and dipicolinic acid. The hexose content of both fractions of the four species was related to heat resistance. Integument fractions consisted chiefly of protein together with variable amounts of the mucopeptide constituents, α, ϵ-diaminopimelic acid (DAP) and hexosamine. In the thermophiles the DAP and hexosamine were found chiefly in the insoluble integuments fractions, while in B. cereus and B. subtilis most of this material was soluble. Integument preparations, containing mainly protein with little mucopeptide, consisted chiefly of outer and inner spore coats, while preparations having more mucopeptide contained also residual cortical material and a cortical membrane (possibly the germ cell wall). The results suggest that spore integuments consist of mainly proteinaceous outer and inner coats together with variable amounts of residual cortex and cortical membrane which contain the mucopeptide material.

Partial Lack of N-Acetyl Substitution of Glucosamine in the Peptidoglycan of the Budding Phototrophic Rhodomicrobium vannielii

1987 ◽  
Vol 42 (11-12) ◽  
pp. 1165-1170 ◽  
Author(s):  
Uwe J. Jürgens ◽  
Baldur Rieth ◽  
Jürgen Weckesser ◽  
Crawford S. Dow ◽  
Wilfried A. König
Keyword(s):  
Fatty Acids ◽  
Content Analysis ◽  
Type Structure ◽  
Diaminopimelic Acid ◽  
Strain Atcc ◽  
Muramic Acid ◽  
Cross Linkage ◽  
Rigid Layer ◽  
Rhodomicrobium Vannielii

The rigid layer and peptidoglycan fractions from two strains (ATCC 17100 and Rm 5) of the budding phototrophic Rhodomicrobium vannielii were isolated. Rigid layers of both strains contain protein in addition to peptidoglycan. They were free of polysaccharides and fatty acids. The respective peptidoglycan fractions contain glucosamine, muramic acid, ʟ-and ᴅ-alanine, ᴅ-glutamic and meso-diaminopimelic acid in approximately equimolar ratios except for a signifi­ cant lower relative ᴅ-alanine content. Analysis of partial acid hydrolysates revealed A 1 γ-type structure of Rhodomicrobium vannielii peptidoglycan (shown with strain ATCC 17100). An about 10-30% lack of N-acetylation of glucosamine was indicated. The degree of cross-linkage was found to be about 60% . No differences in peptidoglycan composition and degree of cross-linkage were found between swarmer-and chain-cells as examined with strain Rm 5.

scholarly journals The extraction of cell walls of Pseudomonas aeruginosa with aqueous phenol. The insoluble residue and material from the aqueous layers

1967 ◽  
Vol 105 (2) ◽  
pp. 759-765 ◽  
Author(s):  
K. Clarke ◽  
G. W. Gray ◽  
D. A. Reaveley
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cell Wall ◽  
Cell Walls ◽  
Lipid A ◽  
Diaminopimelic Acid ◽  
Insoluble Residue ◽  
Muramic Acid ◽  
Gram Negative ◽  
Gram Negative Organisms ◽  
Residue Fraction

1. The insoluble residue and material present in the aqueous layers resulting from treatment of cell walls of Pseudomonas aeruginosa with aqueous phenol were examined. 2. The products (fractions AqI and AqII) isolated from the aqueous layers from the first and second extractions respectively account for approx. 25% and 12% of the cell wall and consist of both lipopolysaccharide and muropeptide. 3. The lipid part of the lipopolysaccharide is qualitatively similar to the corresponding material (lipid A) from other Gram-negative organisms, as is the polysaccharide part. 4. The insoluble residue (fraction R) contains sacculi, which also occur in fraction AqII. On hydrolysis, the sacculi yield glucosamine, muramic acid, alanine, glutamic acid and 2,6-diaminopimelic acid, together with small amounts of lysine, and they are therefore similar to the murein sacculi of other Gram-negative organisms. Fraction R also contains substantial amounts of protein, which differs from that obtained from the phenol layer. 5. The possible association or aggregation of lipopolysaccharide, murein and murein sacculi is discussed.

scholarly journals Tracer studies on the biosynthesis of amino acids from lactate by Peptostreptococcus elsdenii

1967 ◽  
Vol 105 (1) ◽  
pp. 299-310 ◽  
Author(s):  
H. J. Somerville ◽  
J. L. Peel
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Tricarboxylic Acid Cycle ◽  
Carbon Chain ◽  
Tricarboxylic Acid ◽  
Diaminopimelic Acid ◽  
Reaction Sequence ◽  
Tracer Studies ◽  
Cell Fractions

Peptostreptococcus elsdenii, a strict anaerobe from the rumen, was grown on a medium containing yeast extract and [1−14C]- or [2−14C]-lactate. Radioisotope from lactate was found in all cell fractions, but mainly in the protein. The label in the protein fraction was largely confined to a few amino acids: alanine, serine, aspartic acid, glutamic acid and diaminopimelic acid. The alanine, serine, aspartic acid and glutamic acid were separated, purified and degraded to establish the distribution of 14C from lactate within the amino acid molecules. The labelling patterns in alanine and serine suggested their formation from lactate without cleavage of the carbon chain. The pattern in aspartic acid suggested formation by condensation of a C3 unit derived directly from lactate with a C1 unit, probably carbon dioxide. The distribution in glutamic acid was consistent with two possible pathways of formation: (a) by the reactions of the tricarboxylic acid cycle leading from oxaloacetate to 2-oxoglutarate, followed by transamination; (b) by a pathway involving the reaction sequence 2 acetyl-CoA→crotonyl-CoA→glutaconate→glutamate.

scholarly journals Human Innate Immune Cells Respond Differentially to Poly-γ-Glutamic Acid Polymers from Bacillus anthracis and Nonpathogenic Bacillus Species

2020 ◽  
Vol 204 (5) ◽  
pp. 1263-1273 ◽  
Author(s):  
Tanya M. Jelacic ◽  
Wilson J. Ribot ◽  
Jennifer Chua ◽  
Anne E. Boyer ◽  
Adrian R. Woolfitt ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Bacillus Anthracis ◽  
Immune Cells ◽  
Innate Immune ◽  
Bacillus Species ◽  
Innate Immune Cells

scholarly journals Comparative Genome Analysis of Bacillus sporothermodurans with Its Closest Phylogenetic Neighbor, Bacillus oleronius, and Bacillus cereus and Bacillus subtilis Groups

2020 ◽  
Vol 8 (8) ◽  
pp. 1185
Author(s):  
Rodney Owusu-Darko ◽  
Mushal Allam ◽  
Arshad Ismail ◽  
Carlos A. S. Ferreira ◽  
Sílvia D. de Oliveira ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Resistance ◽  
Genome Analysis ◽  
Bacillus Species ◽  
Whole Genome ◽  
Comparative Genome Analysis ◽  
Genome Sequences ◽  
Comparative Genome ◽  
P Gene ◽  
Phylogenetic Neighbor

Bacillus sporothermodurans currently possesses one of the most highly heat-resistant spores (HRS), which can withstand ultra-high temperature (UHT) processing. Determination of multiple whole genome sequences of B. sporothermodurans provided an opportunity to perform the first comparative genome analysis between strains and with B. oleronius, B. cereus, and B. subtilis groups. In this study, five whole genome sequences of B. sporothermodurans strains, including those belonging to the HRS clone (SAD and BR12) normally isolated from UHT milk, were compared with the aforementioned Bacillus species for gene clusters responsible for heat resistance. In the phylogenomic analysis, B. sporothermodurans, with its closest phylogenetic neighbor, B. oleronius, clustered with B. thermoamylovorans and B. thermotolerans. Heat shock proteins GrpE, GroES, GroEL, and DnaK presented identical sequences for all B. sporothermodurans strains, indicating that differences in functional efficiency are not involved in the thermal resistance variations. However, comparing all species evaluated, B. sporothermodurans exhibited a different gene configuration in the chromosomal region of the heat shock protein GrpE. Furthermore, only B. sporothermodurans strains presented the stage II sporulation protein P gene located in this region. Multisequence alignment and phylogenetic analysis of the ClpB protein showed differences for HRS and non-HRS strains. The study identified ClpC, ClpE, and ClpX as the three ATPases putatively involved in protein disaggregation in B. sporothermodurans. Bacillussporothermodurans exhibits high homology with other Bacillus species in the DnaK, DnaJ, GroEL, and GroES cluster of genes involved in heat resistance. The data presented here pave the way to select and evaluate the phenotypic effects of genes putatively involved in heat resistance.

scholarly journals Covalent Linkage of Polyamines to Peptidoglycan inAnaerovibrio lipolytica

2000 ◽  
Vol 182 (4) ◽  
pp. 1154-1157 ◽  
Author(s):  
Takashi Hirao ◽  
Masahide Sato ◽  
Akira Shirahata ◽  
Yoshiyuki Kamio
Keyword(s):  
Glutamic Acid ◽  
Anaerobic Bacterium ◽  
Diaminopimelic Acid ◽  
Molar Ratio ◽  
Carboxyl Group ◽  
Strictly Anaerobic ◽  
Amino Group ◽  
Peptide Fragments ◽  
Covalent Linkage ◽  
Glutamic Acid Residue

ABSTRACT Spermidine and cadaverine were found to be constituents of the cell wall peptidoglycan of Anaerovibrio lipolytica, a strictly anaerobic bacterium. The peptidoglycan was degraded with theN-acetylmuramyl-l-alanine amidase and endopeptidase into two peptide fragments, peptide I and peptide II, at a molar ratio of 4:1. Peptides I and II were identified asl-alanine–d-glutamic acid(αcadaverine)γ meso-diaminopimelic acid (DAP)–d-alanine andl-alanine–d-glutamic acid(αspermidine)γ meso-DAP–d-alanine, respectively. The N1-amino group of spermidine was linked to the α-carboxyl group of the d-glutamic acid residue of peptide II.

scholarly journals Modification of the Structure of Peptidoglycan Is a Strategy To Avoid Detection by Nucleotide-Binding Oligomerization Domain Protein 1

2006 ◽  
Vol 75 (2) ◽  
pp. 706-713 ◽  
Author(s):  
Margreet A. Wolfert ◽  
Abhijit Roychowdhury ◽  
Geert-Jan Boons
Keyword(s):  
Carboxylic Acid ◽  
Glutamic Acid ◽  
Synergistic Effects ◽  
Muramyl Dipeptide ◽  
Nucleotide Binding ◽  
Diaminopimelic Acid ◽  
Dependent Manner ◽  
Necrosis Factor Alpha ◽  
Tnf Α ◽  
Oligomerization Domain

ABSTRACT Nucleotide-binding oligomerization domain (NOD) protein 1 (NOD1) and NOD2 are pathogen recognition receptors that sense breakdown products of peptidoglycan (PGN) (muropeptides). It is shown that a number of these muropeptides can induce tumor necrosis factor alpha (TNF-α) gene expression without significant TNF-α translation. This translation block is lifted when the muropeptides are coincubated with lipopolysaccharide (LPS), thereby accounting for an apparently synergistic effect of the muropeptides with LPS on TNF-α protein production. The compounds that induced synergistic effects were also able to activate NF-κB in a NOD1- or NOD2-dependent manner, implicating these proteins in synergistic TNF-α secretion. It was found that a diaminopimelic acid (DAP)-containing muramyl tetrapeptide could activate NF-κB in a NOD1-dependent manner, demonstrating that an exposed DAP is not essential for NOD1 sensing. The activity was lost when the α-carboxylic acid of iso-glutamic acid was modified as an amide. However, agonists of NOD2, such as muramyl dipeptide and lysine-containing muramyl tripeptides, were not affected by amidation of the α-carboxylic acid of iso-glutamic acid. Many pathogens modify the α-carboxylic acid of iso-glutamic acid of PGN, and thus it appears this is a strategy to avoid recognition by the host innate immune system. This type of immune evasion is in particular relevant for NOD1.

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