Complement-activating protein M161Ag is a Mycoplasma fermentans gene product that induces cytokine production by human monocytes

Matsumoto, Masayuki; Kikkawa, Satomi; Nishiguchi, Miyuki; Nishimura, Hidekazu; Seya, Tsukasa

doi:10.1016/s0161-5890(98)90817-3

Cited by 16 publications

(29 citation statements)

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“…The profile of the LAMP fraction of Mycoplasma fermentans revealed 29, 38, 41, 61, 78, 95 and 150 kDa proteins. The bands p35 and p29 identified in this study are those referred in the literature as being specific for M. penetrans and M. fermentans (7,15,27) (Fig. 1).…”

Section: Resultssupporting

confidence: 70%

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Characterization of Mycoplasma penetrans and Mycoplasma fermentans immunodominant proteins

Bruder

Godry

Takei

et al. 2005

Braz. J. Microbiol.

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Mycoplasmas are a heterogeneous group of the smallest organisms capable of self replication and are known to cause many detrimental diseases in both animals and humans. These wall-less prokaryotes are enveloped by a lipoprotein membrane and their small genomes are sufficient to synthesize molecules required for growth and self-replication. Among sixteen species isolated from humans, Mycoplasma pneumoniae, an agent of primary atypical pneumonia, and the urogenital tract species Mycoplasma hominis, Ureaplasma urealyticum and Ureaplasma parvum have been confirmed to be pathogenic. Mycoplasma penetrans and Mycoplasma fermentans, which are species associated with HIV, have been investigated mainly in research laboratories. In this study we have characterized lipid-associated membrane proteins (LAMP) of Mycoplasma penetrans and Mycoplasma fermentans, in view of the importance of mycoplasmas in human diseases and the peculiar antigenic variation observed in these species. To characterize proteins with possible diagnostic value, we used ELISA and Western blot in sera of pregnant women whose cervical samples were positive for these species of mycoplasmas when tested by PCR. ELISA showed IgG anti-LAMP-M. fermentans antibodies to be present in 57.5% of cases and IgM antibodies to be present in 74.5% of cases. The three samples that were PCR positive for M. penetrans showed IgG anti-LAMP-M. penetrans antibodies, and one sample was positive for IgM. No IgA antibodies against either species were detected in any of the samples. LAMP analysis by Western blot revealed the 35, 38, 42, 61 and 103 kDa proteins of M. penetrans and the 29, 38, 41, 61, 78 and 95 kDa proteins of M. fermentans. Among these, will be considered p35 to M. penetrans and 29 kDa protein to M. fermentans, the main immunoreactive proteins and therefore useful markers for further laboratory diagnosis.

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Section: Resultssupporting

confidence: 70%

“…The antigenic variation in these species is clearly demonstrated by the presence of p150, p 95, p78, p61, p48, p43, p41, p38 and p29 proteins. Protein p29 is the main lipid-associated membrane protein and expresses a high frequency of phase variation (15,25).…”

Section: Introductionmentioning

confidence: 99%

Characterization of Mycoplasma penetrans and Mycoplasma fermentans immunodominant proteins

Bruder

Godry

Takei

et al. 2005

Braz. J. Microbiol.

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“…Anti-CD83 mAb was purchased from Cosmo Bio (Tokyo, Japan), anti-CD86 mAb was from Ancell (Bayport, MN), and FITC-labeled anti-mouse IgG was from American Qualex Abs (San Clemente, CA). M161Ag was purified from an infected human cell line P39 ϩ , as described (31). A synthetic lipopeptide based upon the full-length MALP-2 (sMALP-2) was prepared using dipalmitoyl-S-glyceryl cysteine, as described (29).…”

Section: Cells and Reagentsmentioning

confidence: 99%

“…It possesses a unique NH 2 -terminal lipoamino acid, S-diacylglyceryl cysteine, followed by 403 aa, including five tryptophan residues encoded by TGA codons (31,33). Biosynthetic labeling of cells revealed the palmitoylation of M161Ag (31).…”

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confidence: 99%

Mycoplasma fermentansLipoprotein M161Ag-Induced Cell Activation Is Mediated by Toll-Like Receptor 2: Role of N-Terminal Hydrophobic Portion in its Multiple Functions

Nishiguchi

Matsumoto

Takao

et al. 2001

The Journal of Immunology

114

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M161Ag is a 43-kDa surface lipoprotein of Mycoplasma fermentans, serving as a potent cytokine inducer for monocytes/macrophages, maturing dendritic cells (DCs), and activating host complement on affected cells. It possesses a unique N-terminal lipo-amino acid, S-diacylglyceryl cysteine. The 2-kDa macrophage-activating lipopeptide-2 (MALP-2), recently identified as a ligand for Toll-like receptor 2 (TLR2), is derived from M161Ag. In this study, we identified structural motifs sustaining the functions of M161Ag using wild-type and unlipidated rM161Ag with (SP+) or without signal peptides (SP−). Because the SP+ rM161Ag formed dimers via 25Cys, we obtained a monomeric form by mutagenesis (SP+C25S). Only wild type accelerated maturation of human DCs as determined by the CD83/86 criteria, suggesting the importance of the N-terminal fatty acids for this function. Wild-type and the SP+ form of monomer induced secretion of TNF-α and IL-12 p40 by human monocytes and DCs. Either lipid or signal peptide at the N-terminal portion of monomer was required for expression of this function. In contrast, murine macrophages produced TNF-α in response to wild type, but not to any recombinant form of M161Ag, suggesting the species-dependent response to rM161Ag. Wild-type and both monomeric and dimeric SP+ forms possessed the ability to activate complement via the alternative pathway. Again, the hydrophobic portion was associated with this function. These results, together with the finding that macrophages from TLR2-deficient mice did not produce TNF-α in response to M161Ag, infer that the N-terminal hydrophobic structure of M161Ag is important for TLR2-mediated cell activation and complement activation.

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“…MoAbs against human cytomegalovirus (HCMV) early antigen and against gp120 of HIV were generous gifts from Dr K. Kondo (Osaka University, Japan). A MoAb against M161Ag (MK53), a mycoplasma product that induces homologous C activation, was prepared in our laboratory [29]. MoAbs against C3b and C3bi were gifts from Dr K. Iida …”

Section: Serum Antibodies and Reagentsmentioning

confidence: 99%

Antibody-independent classical complement pathway activation and homologous C3 deposition in xeroderma pigmentosum cell lines

Kurita

Matsumoto

Tsuji

et al. 1999

Clinical and Experimental Immunology

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SUMMARYOf human malignantly transformed cell lines, xeroderma pigmentosum (XP) cell lines were found to be highly susceptible to homologous complement (C): cells were opsonized by C3 fragments on incubation with diluted normal human serum. C3 fragment deposition on XP cells was Ca 2 -dependent and occurred on live cells but not UV-irradiated apoptotic cells. (Ca 2 is required for activation of the classical C pathway via C1q and the lactin pathway via mannose binding lectin (MBL), and the surface of apoptotic cells usually activates the alternative C pathway.) In this study we tested which of the pathways participates in XP cell C3 deposition. In seven cell lines that allowed C3 deposition (i), Clq was shown to be essential but MBL played no role in C activation, (ii) Cls but not MASP bound XP cells for activation, (iii) no antibodies recognizing XP cells were required for homologous C3 deposition, and (iv) the alternative pathway barely participated in C3 deposition. Furthermore, the levels of Cregulatory proteins for host cell protection against C, decay-accelerating factor (DAF, CD55) and membrane cofactor protein (MCP, CD46), were found to be relatively low in almost all XP cell lines compared with normal cells. These results indicate that XP cells activate the classical C pathway in an antibody-independent manner through the expression of a molecule which directly attracts C1q in a Cactivating form, and that relatively low levels of DAF and MCP on XP cells facilitate effective C3 deposition. The possible relationship between the pathogenesis of XP and our ®ndings is discussed.

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Complement-activating protein M161Ag is a Mycoplasma fermentans gene product that induces cytokine production by human monocytes

Cited by 16 publications

References 0 publications

Characterization of Mycoplasma penetrans and Mycoplasma fermentans immunodominant proteins

Characterization of Mycoplasma penetrans and Mycoplasma fermentans immunodominant proteins

Mycoplasma fermentansLipoprotein M161Ag-Induced Cell Activation Is Mediated by Toll-Like Receptor 2: Role of N-Terminal Hydrophobic Portion in its Multiple Functions

Antibody-independent classical complement pathway activation and homologous C3 deposition in xeroderma pigmentosum cell lines

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