Structures and Biological Activities of Peptidoglycans of Listeria monocytogenes and Propionibacterium acnes12

Kamisango, Keiichi; Saiki, Ikuo; Tanio, Yoshiro; Okumura, Hiroyuki; Araki, Yoshio; Sekikawa, Isao; Azuma, Ichiro; Yamamura, Yuichi

doi:10.1093/oxfordjournals.jbchem.a133918

Cited by 78 publications

(40 citation statements)

References 7 publications

(8 reference statements)

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“…The partial hydrolysate of the peptidoglycans of P. technicum, P. avidum, P. granulosum, and C. parvum contained several peptides and saccharides, namely AlaGlu, Glu-Agpm, A 2pm-Gly, A 2pm-Ala, Ala-Glu-Ajpm, GlcN-Mur-Ala, and GlcN-Mur, which were similar to those of P. acnes (9). In the case of the peptidoglycans of P. jreudenreichii and P. shermanii, the peptides Ala-Glu, Glu-Ajpm, …”

Section: B)mentioning

confidence: 82%

Structures of Peptidoglycans of Propionibacterium

Kamisango

Fujii

Yanagihara

et al. 1983

Microbiology and Immunology

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Certain anaerobic coryneforms such as Propionibacterium acnes and Propionibacterium granulosum have been shown to have potent adjuvant and antitumor activities in experimental systems (I, 6, 10). In our previous papers, it was shown that the cell walls of P. acnes, P. granulosum, and P. avidum are adjuvants and antitumor agents (5), and that the peptidoglycan of P. acnes plays an important role in these biological activities (9).Recently, the anaerobic "Corynebacterium" species were classified as Propionibacterium (4,8), and a few studies on the biochemical taxonomy of Propionibacterium were carried out (II, 12). We have reported that the peptidoglycan of P. acnes contains glycine in two different linkages, and should be classified as a new type (9). In the present work, we studied the chemical composition and the structure of peptidoglycans of various species of Propionibacterium and C. paroum for their biochemical taxonomy.The strains of Propionibacterium freudenreichii IFO 12424, Propionibacterium shermanii IFO 12426, and Propionibacterium technicum IFO 12428 were kindly supplied by the Institute for Fermentation, Osaka. The cells were anaerobically cultured at 30 C for 4 days in thioglycollate medium (Eiken Kagaku Co., Ltd.), killed by heating at 80 C for I hr, collected by centrifugation and washed with water three times. The cells of Propionibacterium avidum ATCC 25577, Propionibacterium granulosum ATCC 24464, and Propionibacterium acnes C7 were prepared as described previously (5). The cells of Corynebacterium parvum 1M 1585 were kindly supplied by Kissei Pharmaceutical Co., Ltd. The cell walls of P. freudenreichii and other bacteria were prepared by a method similar to that described previously (9). Peptidoglycans were obtained from the cell walls by treatment with 5% trichloroacetic acid at 60 C for 24 hr. Other materials and methods used in this study were described previously (9).The amino acid and amino sugar composition of peptidoglycans of Propionibacterium and C. parvum are summarized in Table I. The peptidoglycans of P. freudenreichii and P. shermanii were composed of glutamic acid, alanine, diaminopimelic acid, muramic acid, and glucosamine. On the other hand, the constituents 635

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Section: B)mentioning

confidence: 82%

Structures of Peptidoglycans of Propionibacterium

Kamisango

Fujii

Yanagihara

et al. 1983

Microbiology and Immunology

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“…The resistance to degradation was attributed to the unique structure of the peptidoglycan (PGN) component, which has been identified as the active principle of cell wall skeleton preparations of P. acnes (40,41). At present it is not known whether the unique structure of P. acnes PGN is responsible for the TLR9-mediated effects.…”

Section: Discussionmentioning

confidence: 99%

Requirement for TLR9 in the Immunomodulatory Activity of Propionibacterium acnes

Kalis

Gumenscheimer

Freudenberg

et al. 2005

The Journal of Immunology

117

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Propionibacterium acnes (formerly Corynebacterium parvum) is part of the human flora and, as such, is associated with several human pathologies. It possesses strong immunomodulatory activities, which makes this bacterium interesting for prophylactic and therapeutic vaccination. The bacterial component(s) and the host receptor(s) involved in the induction of these activities are poorly understood. We show in this study that TLR9 is crucial in generating the characteristic effects of killed P. acnes priming in the spleen, such as extramedullary hemopoiesis and organ enlargement, and granuloma formation in the liver. Furthermore, the ability to overproduce TNF-α and IFN-γ in response to LPS, lipid A, synthetic lipopeptide Pam3CysK4, or whole killed bacteria was present in P. acnes-primed wild-type, but not TLR9−/−, mice. Finally, P. acnes priming failed to induce enhanced resistance to murine typhoid fever in TLR9−/− mice. Thus, TLR9 plays an essential role in the induction of immunomodulatory effects by P. acnes. Because IFN-γ is a key mediator of these effects, and enhanced IFN-γ mRNA expression was absent in spleen and liver of P. acnes-primed TLR9−/− mice, we conclude that TLR9 is required for the induction of IFN-γ by P. acnes.

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“…It is a polymer of alternating units of the disaccharide N-acetylmuramic acid (MurNAc)-(␤-1,4)-Nacetylglucosamine (GlcNAc), cross-linked by peptidic bridges. Muropeptides, which in L. monocytogenes are L-alanyl-␥-Dglutamyl-meso-diaminopimelyl-D-alanine-D-alanine, are bound to the MurNAc residue and are connected by a direct link between the D-Ala residue of one lateral peptide and the mesodiaminopimelyl residue of the other stem peptide (44,57,89,162). Partial deacetylation of GlcNAc residues by PgdA enzyme is another characteristic of Listeria peptidoglycan (21,89) (see below).…”

Section: Peptidoglycanmentioning

confidence: 99%

Listeria monocytogenesSurface Proteins: from Genome Predictions to Function

Bierne

Cossart

2007

Microbiol Mol Biol Rev

210

257

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SUMMARY The genome of the human food-borne pathogen Listeria monocytogenes is predicted to encode a high number of surface proteins. This abundance likely reflects the ability of this bacterium to survive in diverse environments, including soil, food, and the human host. This review focuses on the various mechanisms by which listerial proteins are attached at the bacterial surface and their many functions, including peptidoglycan metabolism, protein processing, adhesion to host cells, and invasion of host tissues. Extensive in silico analysis of the domains or motifs present in these mosaic proteins reveals that diverse structural features allow the surface proteome to interact with diverse bacterial or host components. This diversity offers new clues about the molecular bases of Listeria pathogenesis.

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Structures and Biological Activities of Peptidoglycans of Listeria monocytogenes and Propionibacterium acnes12

Cited by 78 publications

References 7 publications

Structures of Peptidoglycans of Propionibacterium

Structures of Peptidoglycans of Propionibacterium

Requirement for TLR9 in the Immunomodulatory Activity of Propionibacterium acnes

Listeria monocytogenesSurface Proteins: from Genome Predictions to Function

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