399 research outputs found

    Twin SLS-Like Peptides of Beta-Hemolytic S. anginosus

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    Streptococcus anginosus is a member of the anginosus group streptococci, which form part of the normal human oral flora. In contrast to the pyogenic group streptococci, our knowledge of the virulence factors of the anginosus group streptococci, including S. anginosus, is not sufficient to allow a clear understanding of the basis of their pathogenicity. Generally, hemolysins are thought to be important virulence factors in streptococcal infections. In the present study, a sag operon homologue was shown to be responsible for beta-hemolysis in S. anginosus strains by random gene knockout. Interestingly, contrary to pyogenic group streptococci, beta-hemolytic S. anginosus was shown to have two tandem sagA homologues, encoding streptolysin S (SLS)-like peptides, in the sag operon homologue. Gene deletion and complementation experiments revealed that both genes were functional, and these SLS-like peptides were essential for beta-hemolysis in beta-hemolytic S. anginosus. Furthermore, the amino acid sequence of these SLS-like peptides differed from that of the typical SLS of S. pyogenes, especially in their propeptide domain, and an amino acid residue indicated to be important for the cytolytic activity of SLS in S. pyogenes was deleted in both S. anginosus homologues. These data suggest that SLS-like peptides encoded by two sagA homologues in beta-hemolytic S. anginosus may be potential virulence factors with a different structure essential for hemolytic activity and/or the maturation process compared to the typical SLS present in pyogenic group streptococci

    Rapid screening method for detecting highly pathogenic Streptococcus intermedius strains carrying a mutation in the lacR gene

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    Streptococcus intermedius is a member of the normal human commensal flora and secretes a human-specific cytolysin intermedilysin (ILY) as a major virulence factor. Expression of ily is repressed by LacR and loss-of-function mutations of LacR are observed in many ILY high-producing strains isolated from deep-seated abscesses, suggesting that high ILY production is necessary for increased virulence. However, because ILY exhibits no β-hemolysis on animal blood agar plates, differentiating ILY high- and low-producing strains using conventional laboratory methods is not possible. Interestingly, S. intermedius also produces glycosidases, including MsgA and NanA, which exhibit N-acetyl-β-D-glucosaminidase and neuraminidase activities, respectively. Moreover, MsgA expression, but not NanA, is negatively regulated by LacR. Here we measured the activities of MsgA, NanA and ILY in strains isolated from clinical specimens and dental plaque to determine the correlation between these glycosidase activities and ILY hemolytic activity. Hemolytic activity showed a strong positive correlation with MsgA and a weak negative correlation with NanA activities. Therefore, we calculated the ratio of MsgA and NanA activity (M/N ratio). This value showed a stronger positive correlation (r = 0.81) with ILY hemolytic activity and many strains with high M/N ratios (> 2) were ILY high-producers with loss-of-function mutations in LacR.Rapid screening method for highly pathogenic S. intermedius strains based on the ratio of activities of MsgA and NanA resulting from lacR mutations

    Reversible Electric-Field-Driven Magnetic Domain-Wall Motion

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    Control of magnetic domain-wall motion by electric fields has recently attracted scientific attention because of its potential for magnetic logic and memory devices. Here, we report on a new driving mechanism that allows for magnetic domain-wall motion in an applied electric field without the concurrent use of a magnetic field or spin-polarized electric current. The mechanism is based on elastic coupling between magnetic and ferroelectric domain walls in multiferroic heterostructures. Pure electric-field-driven magnetic domain-wall motion is demonstrated for epitaxial Fe films on BaTiO3 with in-plane and out-of-plane polarized domains. In this system, magnetic domain-wall motion is fully reversible and the velocity of the walls varies exponentially as a function of out-of-plane electric-field strength.Peer reviewe

    Alternating domains with uniaxial and biaxial magnetic anisotropy in epitaxial Fe films on BaTiO[sub 3]

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    We report on domain formation and magnetization reversal in epitaxial Fe films on ferroelectric BaTiO3 substrates with ferroelastica–c stripe domains. The Fe films exhibit biaxial magnetic anisotropy on top of c domains with out-of-plane polarization, whereas the in-plane lattice elongation of a domains induces uniaxial magnetoelasticanisotropy via inverse magnetostriction. The strong modulation of magnetic anisotropy symmetry results in full imprinting of the a–c domain pattern in the Fe films. Exchange and magnetostaticinteractions between neighboring magnetic stripes further influence magnetization reversal and pattern formation within the a and c domains.Peer reviewe

    Heterologous co-chaperone recognition

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    Streptococcus intermedius DnaK complements the temperature-sensitive phenotype of an Escherichia coli dnaK null mutant, only if co-chaperones DnaJ and GrpE are co-expressed. Therefore, we examined whether S. intermedius DnaK and E. coli DnaK could recognize heterologous co-chaperones in vitro. The addition of heterologous GrpE to DnaK and DnaJ partially stimulated ATPase activity, and almost completely stimulated the luciferase refolding activity. Addition of heterologous DnaJ to GrpE and DnaK also stimulated ATPase activity but significant luciferase refolding activity was not observed. Moreover, E. coli DnaJ had a negative effect on the luciferase refolding activity of the S. intermedius DnaK chaperone system. In E. coli chaperone mutants, with the exception of E. coli DnaJ higher expression of the heterologous co-chaperones partially or almost completely complemented the temperature-sensitive-phenotype. These results indicated that all heterologous co-chaperones could at least partially recognize DnaK of a distantly related species. A region of the ATPase domain that is present in the DnaK of gram-negative bacteria is absent in the DnaK of gram-positive bacteria. This region is believed to be important for the recognition of co-chaperones from gram-negative bacteria. However, insertion of this segment into the S. intermedius DnaK failed to increase its ability to recognize E. coli co-chaperones. This implied that this region might be unnecessary or insufficient for the recognition of E. coli co-chaperones. Therefore, our data suggested that a basic structural similarity is conserved among the components of the S. intermedius and E. coli DnaK chaperone systems, which allow weak associations between heterologous components

    Strong confinement of PbSe and PbS quantum dots

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    We synthesized PbSe and PbS quantum dots in strong-confinement regime, and measured energy relaxation time by using pump-and-probe experiments. Energy relaxation time of PbSe dots in phosphate glasses showed clear correlation with the average radius. Smaller dots were shown to have shorter decay times. This dependence is ascribed to the relaxation to the surface of the dots

    1+1 dimensional QCD with fundamental bosons and fermions

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    We analyze the properties of mesons in 1+1 dimensional QCD with bosonic and fermionic ``quarks'' in the large \nc limit. We study the spectrum in detail and show that it is impossible to obtain massless mesons including boson constituents in this model. We quantitatively show how the QCD mass inequality is realized in two dimensional QCD. We find that the mass inequality is close to being an equality even when the quarks are light. Methods for obtaining the properties of ``mesons'' formed from boson and/or fermion constituents are formulated in an explicit manner convenient for further study. We also analyze how the physical properties of the mesons such as confinement and asymptotic freedom are realized.Comment: 20 pages, harvmac, 5 figure

    Do teashirt family genes specify trunk identity? Insights from the single tiptop/teashirt homolog of Tribolium castaneum

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    The Drosophila teashirt gene acts in concert with the homeotic selector (Hox) genes to specify trunk (thorax and abdomen) identity. There has been speculation that this trunk-specifying function might be very ancient, dating back to the common ancestor of insects and vertebrates. However, other evidence suggests that the role of teashirt in trunk identity is not well conserved even within the Insecta. To address this issue, we have analyzed the function of Tc-tiotsh, the lone teashirt family member in the red flour beetle, Tribolium castaneum. Although Tc-tiotsh is important for aspects of both embryonic and imaginal development including some trunk features, we find no evidence that it acts as a trunk identity gene. We discuss this finding in the context of recent insights into the evolution and function of the Drosophila teashirt family genes
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