Immunomodulating and Related Biological Activities of Bacterial Cell Walls and Their Components, Enzymatically Prepared or Synthesized

Kotani, Shozo; Takada, Haruhiko; Tsujimoto, M; Ogawa, Tomohiko; Kato, Kimiko; Okunaga, Takafumi; Ishihara, Y.; Kawasaki, Akinori; Morisaki, Ichijiro; Kono, N; Shimono, Tomoyuki; Shiba, Tetsuo; Kusumoto, Shoichi; Inage, Masaru; Harada, Kazuhiro; Kitaura, Toshiyuki; S, Kano; Inai, Shinya; Nagai, Kazuyoshi; Matsumoto, Misako; Kubo, Takashi; Katô, Masahiko; Tada, Zenichi; Yokogawa, Kanae; Kawata, Seiichi; Inoue, Atsuo

doi:10.1007/978-1-4684-4115-4_15

Cited by 16 publications

(9 citation statements)

References 48 publications

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“…The blocking effect on the classical pathway by the addition of 10 mM EGTA [ethylene glycol-bis(paminoethyl ether)-N,N,N',N'-tetraacetic acid] plus 5 mM MgCl2 was also determined. In the latter assay, a watersoluble peptidoglycan (SEPS), which was prepared from Staphylococcus epidermidis cell walls by using an endopeptidase (16) capable of cleaving cross-linkages to make a polymer of peptidoglycan subunits and was shown to activate human complement system exclusively via the alternative pathway in a previous study (19), was used as a reference.…”

Section: Methodsmentioning

confidence: 99%

“…Oil-induced peritoneal macrophages cultivated as described above were exposed to test materials (medium alone in control culture) for 48 h. The cells were preincubated with 1 ml of 50 ,uM cytochrome c (from horse heart, type VI; Sigma) in HEPES (N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid) buffer at 37°C for and the culture was incubated at 37°C for 15 min. The rate of reduction of cytochrome c in the reaction mixture was measured by recording the A550 to A540 with a double-beam spectrophotometer (model 200-20; Hitachi, Tokyo, Japan) and expressed as nanomoles per minute per 106 cells (molar absorption coefficient, 19.1 x 103).…”

Section: [14c]glucosamine Hydrochloride (New England Nuclearmentioning

confidence: 99%

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Low endotoxic activities of synthetic Salmonella-type lipid A with an additional acyloxyacyl group on the 2-amino group of beta (1-6) glucosamine disaccharide 1,4'-bisphosphate

Kotani

Takada²,

Takahashi

et al. 1986

Infect Immun

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A synthetic lipid A (Salmonella type, compound 516), P(1-6)-linked D-glucosamine disaccharide 1,4'bisphosphate, with three acyloxyacyl groups and one hydroxyacyl group, i.e., (R)-3-hexadecanoyloxytetradecanoyl, (R)-3-hydroxytetradecanoyl, (R)-3-dodecanoyloxytetradecanoyl, and (R)-3-tetradecanoyloxytetradecanoyl groups at the 2-amino, 3-hydroxyl, 2'-amino, and 3'-hydroxyl groups, respectively, was less biologically active than the synthetic Escherichia coli-type lipid A (compound 506), which has only two acyloxyacyl groups at the 2' and 3' positions and is substituted with a (R)-3-hydroxytetradecanoyl group at the 2-amino group. Compound 516 exhibited considerably weaker pyrogenic and leukopenic activity than compound 506, and it scarcely prepared rabbit skin for the Shwartzman reaction and lacked lethal toxicity on chicken embryos, although its lethal toxicity in galactosamine-loaded mice was as strong as that of compound 506. Compound 516 was also less active than compound 506 or natural E. coli lipid A (from Restrain F515) in other biological test systems, such as the Limulus test, stimulation of macrophages and lymphocytes, and interferon-inducing activity but not for interleukin-1 induction or complement activation. This observation suggests that there is an optimal number of acyloxyacyl groups on the glucosamine backbone for producing the biological activities of lipid A, especially the endotoxic activities. The 4'-monophosphate analog (compound 514) of compound 516 in general had significantly weaker activity than compound 516 in the above assays, most probably because of its greater hydrophobicity and consequently lower solubility in assay systems. Bacterial R595 lipid A derived from S. minnesota Re-mutant, which is a mixture of compounds 516 and 506, their 4'-monophosphate analogs and other compounds, exerted intermediate degrees of activity between compounds 506 and 516 in the various test systems employed. We (20) previously reported the synthesis of a lipid A with biological activities -comparable to those of a natural lipid A, which is responsible for the endotoxic and most of the other biological activities of bacterial lipopolysaccharides (LPS) (7,21,38). A synthetic compound (compound 506), P(1-6)linked D-glucosamine disaccharide 1,4'-bisphosphate, having two (R)-3-hydroxytetradecanoyl groups, the (R)-3dodecanoyloxytetradecanoyl, and the (R)-3-tetradecanoyloxytetradecanoyl group at 2-amino, 3-hydroxyl, 2'-amino and 3'-hydroxyl groups, respectively, which was prepared according to the proposed structure of lipid A from an Escherichia coli Re-mutant (F515) (10, 11; Fig. 1A), exhibited full biological activities identical to or sometimes stronger than those of the reference natural products, F515 lipid A and E. coli 055:B5 LPS.

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Section: Methodsmentioning

confidence: 99%

Section: [14c]glucosamine Hydrochloride (New England Nuclearmentioning

confidence: 99%

Low endotoxic activities of synthetic Salmonella-type lipid A with an additional acyloxyacyl group on the 2-amino group of beta (1-6) glucosamine disaccharide 1,4'-bisphosphate

Kotani

Takada²,

Takahashi

et al. 1986

Infect Immun

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“…For further information, the reader should consult several excellent reviews. In 1981, Kotani and colleagues [27] reviewed their work in Japan with MDP and its derivatives. Yamamura and Azuma [28] reviewed bacterial therapy of cancer from BCG to muramyl peptides.…”

Section: Introductionmentioning

confidence: 99%

Effects of Muramyl Peptides on Macrophages, Monokines, and Sleep

Pabst

Beranová-Giorgianni

Krueger

1999

Neuroimmunomodulation

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Muramyl peptides are fragments of peptidoglycan from the cell walls of bacteria. Because of their unique chemistry, the immune system recognizes that muramyl peptides are products of bacteria, and it responds by becoming activated to resist infection. This resistance to infection is nonspecific, and extends to unrelated species of bacteria, fungi, and viruses. A key mechanism of the resistance to infection is activation of macrophages. Macrophage activation results in increased production of microbicidal oxygen radicals like superoxide and peroxide, and in increased secretion of inflammatory cytokines like interleukin-1β and tumor necrosis factor-α. These cytokines, besides activating neutrophils, B lymphocytes, and T lymphocytes, act on the central nervous system to induce physiological responses like fever and sleep. These physiological responses also aid in combating infection. Muramyl peptides also activate macrophages and other cells of the immune system to kill cancer cells. Muramyl peptides and similar agents will become more important as therapeutic agents in the future, due to increasing resistance of microbes to antibiotics, and increasing numbers of patients with immunodeficiencies.

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“…Part of this work was presented by S. Kotani in the Conferences on "Immunomodulation by Bacteria and Their Products" held on November 18-20, 1979, in Tampa, Florida, and was published in a monograph (20).…”

Section: Discussionmentioning

confidence: 99%

“…On the other hand, the observation that B30-MDP (D-isoAsn) activates complement in a similar way to its parent molecule suggests that the complement activation observed was due to the a-branched, long-chain fatty acid portion of the molecule, not to the muramyl peptide moiety, and that the mechanisms of comple-ment activation by B30-MDP are different from either those of cell wall peptidoglycans or a "polymer" (SEPS) of the peptidoglycan subunits. This may be supported by the fact that B30-MDP(D-isoAsn) is far less active than its parent molecule (B30-MDP) in other immunopharmacological properties (20,21,32). In this context, we would like to add here that the complement cascade in pooled human serum, which had been incubated with a suspension (2 mg/ml) of B30-MDP at 0 C for 45 min and had been centrifuged to remove a complex of B30-MDP and possible "anti-B30-MDP antibody" and excess of B30-MDP, was activated by B30-MDP as by the untreated control serum (data not shown).…”

Section: Discussionmentioning

confidence: 99%

Activation of the Human Complement Cascade by Bacterial Cell Walls, Peptidoglycans, Water‐Soluble Peptidoglycan Components, and Synthetic Muramylpeptides—Studies on Active Components and Structural Requirements

Kawasaki

Takada²,

Kotani

et al. 1987

Microbiology and Immunology

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Cell walls isolated from 29 strains of 24 gram-positive bacterial species, whose peptidoglycans belong to the group A type of Schleifer and Kandler's classification, with one exception (Arthrobacter sp.), were shown to activate the complement cascade in pooled fresh human serum mainly through the alternative pathway and partly through the classical one. The complement-activating effect of cell walls (5 species) possessing group B type peptidoglycan, except those of Corynebacterium insidiosum, was weaker than that of the walls with group A type peptidoglycan. Preparations of peptidoglycan isolated from cell walls of Staphylococcus aureus, Streptococcus pyogenes, and Lactobacillus plantarum also activated the alternative pathway of the complement cascade, but less effectively than the respective parent cell walls. A water-soluble "polymer" of peptidoglycan subunits (SEPS), which was prepared from Staphylococcus epidermidis peptidoglycans by treatment with a cross-bridge degrading endopeptidase, retained most of the complement-activating ability of the parent cell walls. A peptidoglycan "monomer," SEPS-M, which was obtained by hydrolysis of the glycan chain of SEPS with endo-N-acetylmuramidase to disaccharide units did not activate complement. In conformity with this finding, neither synthetic N-acetylmuramyl-L-alanyl-D-isoglutamine (MDP) nor MDP-L-Lys-D-Ala activated the complement cascade. Among several lipophilic derivatives of MDP, 6-and 6-O-(2-tetradecylhexadecanoyl)-MDP (B30-MDP) were shown to activate complement through the alternative as well as the classical pathway and exclusively through the classical pathway, respectively. The finding that a D-isoasparagine 551

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Immunomodulating and Related Biological Activities of Bacterial Cell Walls and Their Components, Enzymatically Prepared or Synthesized

Cited by 16 publications

References 48 publications

Low endotoxic activities of synthetic Salmonella-type lipid A with an additional acyloxyacyl group on the 2-amino group of beta (1-6) glucosamine disaccharide 1,4'-bisphosphate

Low endotoxic activities of synthetic Salmonella-type lipid A with an additional acyloxyacyl group on the 2-amino group of beta (1-6) glucosamine disaccharide 1,4'-bisphosphate

Effects of Muramyl Peptides on Macrophages, Monokines, and Sleep

Activation of the Human Complement Cascade by Bacterial Cell Walls, Peptidoglycans, Water‐Soluble Peptidoglycan Components, and Synthetic Muramylpeptides—Studies on Active Components and Structural Requirements

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