Stimulation of migration of human monocytes by bacterial cell walls and muramyl peptides

Ogawa, Tomohiko; Kotani, Shozo; Fukuda, Kuniko; Tsukamoto, Yoshihiko; Mori, Mayumi; Kusumoto, Shoichi; Shiba, Tetsuo

doi:10.1128/iai.38.3.817-824.1982

Cited by 22 publications

(12 citation statements)

References 43 publications

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“…The assay for enhanced migration of monocytes by test materials was performed with a multiwell chemotaxis assembly (Neuro Probe, Cabin John, Md.) as described previously (24). The number of monocytes that migrated to the surface of the membrane sheet adjacent to the lower well containing an added test specimen was determined in triplicate for each experimental point.…”

Section: Methodsmentioning

confidence: 99%

Immunobiological activities of a porin fraction isolated from Fusobacterium nucleatum ATCC 10953

et al. 1988

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From Fusobacterium nucleatum ATCC 10953 cell envelope fraction whose inner membranes had been removed by treatment with sodium N-lauroyl sarcosinate, an outer membrane protein (37,000 Mr in a native state) was prepared by extraction with lithium dodecyl sulfate. The protein thus obtained showed distinct porin activity, namely, the ability to form hydrophilic diffusion pores by incorporation into the artificial liposome membrane. The porin fraction exhibited strong immunobiological activities in the in vitro assays: B-cell mitogenicity and polyclonal B-cell activation on murine splenocytes, stimulatory effects on guinea pig peritoneal macrophages, and enhancement of the migration of human blood monocytes. The porin fraction also exhibited immunoadjuvant activity to increase the antibody production against sheep erythrocytes in the spleen of mice that were immunized by sheep erythrocytes with porin. Although chemical analyses revealed that the test porin fraction contained a considerable amount of lipopolysaccharide (LPS) (around 12% of the fraction), the studies with LPS-nonresponding C3H/HeJ mice and on the inhibitory effects of polymyxin B strongly suggest that most of the above bioactivities are due to porin protein itself, not to coexistent LPS in the porin fraction.

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Section: Methodsmentioning

confidence: 99%

Immunobiological activities of a porin fraction isolated from Fusobacterium nucleatum ATCC 10953

et al. 1988

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“…Therefore, these synthetic peptide segments are considered to be in addition to the infiammatory peptides derived from bacterial components. We previously demonstrated that //-acetylmuramyl-L-alanyl-D-isoglutamine (MDP), the minimum effective structure responsible for the majority of multifold immunomodulating activities of bacterial cell wall peptidoglycans, also enhanced chemotactic activity of human monocytes in a wide range of doses from 0.001 -1 /.igl ml (2x10-^-2x10"^ M) under the same experimental conditions (9,10).…”

Section: Discussionmentioning

confidence: 99%

“…A^-formyl-methionyl-leucyl-phenylalanine (FMLP) was purchased from Sigma Chemical Co., St. Louis, MO and dis-solved in ethanol at a concentration of 10"^ M. This preparation was stored at -2O''C in 0.5-ml portions. Each portion was thawed before use, diluted to indicated concentrations with the culture medium described below and used as a positive chemoattractant for chemotaxis assays (9).…”

Section: Chemotactic Agentsmentioning

confidence: 99%

“…Test specimens and FMLP were diluted with a mixture of 7 parts of Gey's balanced salt solution (Gibco Laboratories, Grand Island, NY) containing 2% bovine serum albumin (Sigma Chemical Co.) and 20 mM A^-2-hydroxyethylpiperazine-A^'-2-ethanesulfonic acid (HEPES; Sigma Chemical Co.) (Gey's bovine serum albumin, pH 7.0) and 5 parts of gelatin-veronal buffer with 2 M MgCl, and 1 M CaCl, (GVB-+) for monocyte chemotaxis assay (9). This mixture was referred to as Gey BSA-GVB-+.…”

Section: Chemotactic Agentsmentioning

confidence: 99%

“…Peripheral blood mononuclear cells were washed with phosphate-buffered saline (pH 7.0; Biken, Osaka, Japan) and suspended at 5x10^ peripheral blood mononuclear cells per ml of gey's BSA. Migration of monocytes in the peripheral blood mononuclear cell sample was measured by use of a multiwell chemotaxis assembly (Neuro Probe, Cabin John, MD) as described previously by Ogawa et al (9). Wells of the bottom plate were filled with 25 lA of test or reference specimens dissolved in Gey's BSA-GVB-+ .…”

Section: Assay For Migration Of Monocytesmentioning

confidence: 99%

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Chemotaxis of human monocytes by synthetic peptides that mimic segments of Porphyromonas gingivalis fimbrial protein

Ogawa

Ogo

Hamada

1994

Oral Microbiology and Immunology

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Porphyromonas gingivalis strain 381 fimbriae and their synthetic peptide segments were assessed for migration-stimulating activity on human peripheral blood monocytes by multiwell chemotaxis assay. P. gingivalis 381 fimbrial protein was found to markedly enhance migration of human monocytes. The observed increase in monocyte migration occurred mainly directed toward a positive stimulus (chemotaxis). Furthermore, lipopolysaccharides extracted from P. gingivalis 381 were shown to induce chemotaxis and chemokinesis. It was also revealed that the migration of monocytes was increased by specific synthetic peptide segments, FP381(61-80) and FP381(171-185), that correspond to GKTLAEVKALTTELTAENQE and DANYLTGSLTTFNGA, respectively, based on the amino acid sequence of the fimbrial subunit protein proposed by Dickinson et al., and the migration stimulation was ascribed to chemotaxis. Furthermore, within the amino acid sequences, the LTXXLTXXN sequence may play an important role in binding the organisms to monocytes and macrophages and in the induction of migration-stimulating activity.

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Treponemal glycoconjugate inhibits Toll‐like receptor ligand‐induced cell activation by blocking LPS‐binding protein and CD14 functions

2003

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Spirochetes are well-known as causative agents of various chronic infectious diseases. Glycolipids of small-sized Treponema spirochetes have been shown to exhibit immunostimulating activities. In this study, we found that a glycoconjugate preparation obtained from Treponema medium (Tm-Gp), an intermediate-sized oral Treponema seen in subgingival plaque from patients with chronic periodontal diseases, diminished the LPS-induced activation of a human monocytic cell line, while TNF- § -induced activation was unaffected. NF-‹ B activation in Ba/F3 cells expressing murine Toll-like receptor (TLR) 4 and MD-2 was inhibited by Tm-Gp in a CD14/LPS-binding protein (LBP)-dependent manner when stimulated with LPS or its active center lipid A but not when stimulated with Taxol. Tm-Gp blocked the binding of LPS to immobilized CD14 and LBP and inhibited nitric oxide (NO) production by a murine M ¤ cell line following stimulation with peptidoglycan and LPS in the presence of FBS, while NO production in response poly (I:C) RNA or CpG DNA remained unaffected. The inhibitory effects of Tm-Gp seem to be attributable to the lipophilic portion of the glycoconjugate. These results indicate that T. medium contains a glycoconjugate possessing an inhibitory effect on TLR-mediated cell activation through interaction with LBP and CD14.

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Stimulation of migration of human monocytes by bacterial cell walls and muramyl peptides

Cited by 22 publications

References 43 publications

Immunobiological activities of a porin fraction isolated from Fusobacterium nucleatum ATCC 10953

Immunobiological activities of a porin fraction isolated from Fusobacterium nucleatum ATCC 10953

Chemotaxis of human monocytes by synthetic peptides that mimic segments of Porphyromonas gingivalis fimbrial protein

Treponemal glycoconjugate inhibits Toll‐like receptor ligand‐induced cell activation by blocking LPS‐binding protein and CD14 functions

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