Description of manganese nodules and crust collected from the Hakurei Maru Cruise GH74-5, September-October, 1974, in the Eastern Central Pacific Basin

The cores and dredges described in this report were taken on the GH74-5 Expedition in September-October, 1974 by the Geological Survey of Japan from the R/V Hakurei Maru. A total of 36 cores, dredges and submarine camera sites have been visited. The survey conducted an investigation of the manganese deposits in the Eastern Pacific Basin and the East of the Okinawa islands

Defenses against oxidative stress in Neisseria gonorrhoeae and Neisseria meningitidis: Distinctive systems for different lifestyles

Defenses against oxidative stress are crucial for the survival of the pathogens Neisseria meningitidis and Neisseria gonorrhoeae. An Mn(II) uptake system is involved in manganese (Mn)-dependent resistance to superoxide radicals in N. gonorrhoeae. Here, we show that accumulation of Mn also confers resistance to hydrogen peroxide killing via a catalase-independent mechanism. An mntC mutant of N. meningitidis is susceptible to oxidative killing, but supplementation of growth media with Mn does not enhance the organism's resistance to oxidative killing. N. meningitidis is able to grow in the presence of millimolar levels of Mn ion, in contrast to N. gonorrhoeae, whose growth is retarded at Mn concentrations >100 mumol/L, indicating that Mn homeostasis in the 2 species is probably quite different. N. meningitidis superoxide dismutase B plays a role in protection against oxidative killing. However, a sodC mutant of N. meningitidis is no more sensitive to oxidative killing than is the wild type. A cytochrome c peroxidase (Ccp) is present in N. gonorrhoeae but not in N. meningitidis. Investigations of a ccp mutant revealed a role for Ccp in protection against hydrogen peroxide killing. These differences in oxidative defenses in the pathogenic Neisseria are most likely a result of their localization in different ecological niches.

Molecular analysis of the psa permease complex of Streptococcus pneumoniae

The psaBCA locus of Streptococcus pneumoniae encodes a putative ABC Mn2+-permease complex. Downstream of the operon is psaD, which may be co-transcribed and encodes a thiol peroxidase. Previously, there has been discordance concerning the phenotypic impact of mutations in the psa locus, resolution of which has been complicated by differences in mutant construction and the possibility of polar effects. Here, we constructed unmarked, in frame deletion mutants DeltapsaB, DeltapsaC, DeltapsaA, DeltapsaD, DeltapsaBC, DeltapsaBCA and DeltapsaBCAD in S. pneumoniae D39 to examine the role of each gene within the locus in Mn2+ uptake, susceptibility to oxidative stress, virulence, nasopharyngeal colonization and chain morphology. The requirement for Mn2+ for growth and transformation was also investigated for all mutants. Inductively coupled plasma mass spectrometry (ICP-MS) analysis provided the first direct evidence that PsaBCA is indeed a Mn2+ transporter. However, this study did not substantiate previous reports that the locus plays a role in choline-binding protein pro-duction or chain morphology. We also confirmed the importance of the Psa permease in systemic virulence and resistance to superoxide and hydrogen peroxide, as well as demonstrating a role in nasopharyngeal colonization for the first time. Further evi-dence is provided to support the requirement for Mn2+ supplementation for growth and transformation of DeltapsaB, DeltapsaC, DeltapsaA, DeltapsaBC, DeltapsaBCA and DeltapsaBCAD mutants. However, transformation, as well as growth, of the DeltapsaD mutant was not dependent upon Mn2+ supplementation. We also show that, apart from sensitivity to hydrogen peroxide, the DeltapsaD mutant exhibited essentially similar phenotypes to those of the wild type. Western blot analysis with a PsaD antiserum showed that deleting any of the genes upstream of psaD did not affect its expression. However, we found that deleting psaB resulted in decreased expression of PsaA relative to that in D39, whereas deleting both psaB and psaC resulted in at least wild-type levels of PsaA.

Functional expression and characterization of Eehinococcus granulosus thioredoxin peroxidase suggests a role in protection against oxidative damage

A full-length cDNA sequence coding for Echinococcus granulosus thioredoxin peroxidase (EgTPx) was isolated from a sheep strain protoscolex cDNA library by immunoscreening using a pool of sera from mice infected with oncospheres. EgTPx expressed as a fusion protein with glutathione S-transferase (GST) exhibited significant thiol-dependent peroxidase activity that protected plasmid DNA from damage by metal-catalyzed oxidation (MCO) in vitro. Furthermore, the suggested antioxidant role for EgTPx was reinforced in an in vivo assay, whereby its expression in BL21 bacterial cells markedly increased the tolerance and survival of the cells to high concentrations of H2O2 compared with controls. Immunolocalization studies revealed that EgTPx was specifically expressed in all tissues of the protoscolex and brood capsules. Higher intensity of labelling was detected in many, but not all, calcareous corpuscle cells in protoscoleces. The purified recombinant EgTPx protein was used to screen sera from heavily infected mice and patients with confirmed hydatid infection. Only a portion of the sera reacted positively with the EgTPx-GST fusion protein in Western blots, suggesting that EgTPx may form antibody-antigen complexes or that responses to the EgTPx antigen may be immunologically regulated. Recombinant EgTPx may prove useful for the screening of specific inhibitors that could serve as new drugs for treatment of hydatid disease. Moreover, given that TPx from different parasitic phyla were phylogenetically distant from host TPx molecules, the development of antiparasite TPx inhibitors that do not react with host TPx might be feasible. (C) 2003 Elsevier B.V. All rights reserved.

The effects of pre-weaning undernutrition on the expression levels of free radical deactivating enzymes in the mouse brain

A mild degree of undernutrition brought about by restricting the amount of food in the diet is known to alter the life span of an animal. It has been hypothesised that this may be related to the effects of undernutrition on an animals anti-oxidant defense system. We have therefore, used real-time PCR (rt-PCR) techniques to determine the levels of mRNA expression for manganese superoxide dismutase (MnSOD), copper/zinc superoxide dismutase (Cu/ZnSOD), glutathione peroxidase 1 (GPx 1) and catalase in the brains of Quackenbush mice undernourished from conception until 21-post-natal days of age. It was found that 21- and 61-day-old undernourished mice had a deficit in the expression of Cu/ZnSOD in both the cerebellum and forebrain regions compared to age-matched controls. The expression of MnSOD was found to be greater in the cerebellum, but not the forebrain region, of 21-day-old undernourished mice. There were no significant differences in the expression of GPx 1 and catalase between control and undernourished or previously undernourished mice. Our results confirm that undernutrition during the early life of a mouse may disrupt some of the enzymes involved in the anti-oxidant defense systems.

Removal of the N-linked glycan structure from the peanut peroxidase prxPNC2: Influence on protein stability and activity

Lines of transgenic tobacco have been generated that are transformed with either the wild-type peanut peroxidase prxPNC2 cDNA, driven by the CaMV3 5S promoter (designated 35S::prxPNC2-WT) or a mutated PNC2 cDNA in which the asparagine residue (Asn(189)) associated with the point of glycan attachment (Asn(189)) has been replaced with alanine (designated 35S::prxPNC2-M). PCR, using genomic DNA as template, has confirmed the integration of the 35S::prxPNC2-WT and 35::prxPNC2-M constructs into the tobacco genome, and western analysis using anti-PNC2 antibodies has revealed that the prxPNC2-WT protein product (PNC2-WT) accumulates with a molecular mass of 34,670 Da, while the prxPNC2-M protein product (PNC2-M) accumulates with a molecular mass of 32,600 Da. Activity assays have shown that both PNC2-WT and PNC2-M proteins accumulate preferentially in the ionically-bound cell wall fraction, with a significantly higher relative accumulation of the PNC2-WT isoenzyme in the ionically-bound fraction when compared with the PNC2-M isoform. Kinetic analysis of the partially purified PNC2-WT isozyme revealed an affinity constant (apparent K-m) of 11.2 mM for the reductor substrate guaiacol and 1.29 mM for H2O2, while values of 11.9 mM and 1.12 mM were determined for the PNC2-M isozyme. A higher Arrenhius activation energy (E,,) was determined for the PNC2-M isozyme (22.9 kJ mol(-1)), when compared with the PNC2-WT isozyme (17.6 kJ mol(-1)), and enzyme assays have determined that the absence of the glycan influences the thermostability of the PNC2-M isozyme. These results are discussed with respect to the proposed roles of N-linked glycans attached to plant peroxidases. (c) 2005 Elsevier Ltd. All rights reserved.

Phase equilibria in high MgO ferro-manganese and silico-manganese smelting slags

Liquidus isotherms and phase equilibria have been determined experimentally for a pseudo-ternary section of the form MnO-(CaO+MgO)-(SiO2+Al2O3) with a fixed Al-2,O-3,/SiO2, weight ratio of 0.17 and MgO/CaO weight ratio of 0.17 for temperatures in the range 1473-1673 K. The primary phase fields present for the section investigated include manganosite (Mn,Mg,Ca)O; dicalcium silicate alpha-2(Ca,Mg,Mn)O (.) SiO2; merwinite 3CaO(.) ((Mg,Mn)O.2SiO(2); wollastonite [(Ca,Mg,Mn)(OSiO2)-Si-.]; ;tephroite [2(Mn,Mg)O.SiO2]; rhodonite [(Mn,Mg)O. diopside [(CaO,MgO,MnO,Al2O3)(SiO2)-Si-.]; tridymite (SiO2), SiO2] and melilite [2CaO (.) (MgO,MnO,Al2O3).2(SiO2,Al2O3)]. The liquidus temperatures relevant to ferro-manganese and silico-manganese smelting slags have been determined. The liquiclus temperature is shown to be principally dependent on the modified basicity weight ratio (CaO+Mgo)/(SiO2+Al2O3) at low MnO concentrations, and dependent on the mole ratio (CaO+ MgO+MnO)/(SiO2+Al2O3) at higher MnO concentrations.

The effect of manganese on the grain size of commercial AZ31 alloy

The effect of manganese on gain refinement of a commercial AZ31 alloy has been investigated using an Al-60%Mn master alloy splatter as an alloying additive at 730 degrees C in aluminium titanite crucibles. It is shown that grain refinement by manganese is readily achievable in AZ31. Electron microprobe analyses reveal that prior to the addition of extra manganese the majority of the intermetallic particles found in AZ31 are of the AL(8)Mn(5) type. However, after the addition of extra manganese in the range from 0.1% to 0.8%, the predominant group of intermetallic particles changes to the metastable AlMn type. This leads to a hypothesis that the metastable AlMn intermetallic particles are more effective than Al8Mn5 as nucleation sites for magnesium grains. The hypothesis is supported by the observation that a long period of holding at 730 degrees C leads to an increase in grain size, due probably to the transformation of the metastable AlMn to the stable Al8Mn5. The hypothesis has also been used to understand the mechanism of grain refinement by superheating.

Defenses against oxidative stress in Neisseria gonorrhoeae: A system tailored for a challenging environment

Neisseria gonorrhoeae is a host-adapted pathogen that colonizes primarily the human genitourinary tract. This bacterium encounters reactive oxygen and reactive nitrogen species as a consequence of localized inflammatory responses in the urethra of males and endocervix of females and also of the activity of commensal lactobacilli in the vaginal flora. This review describes recent advances in the understanding of defense systems against oxidative stress in N. gonorrhoeae and shows that while some of its defenses have similarities to the paradigm established with Escherichia coli, there are also some key differences. These differences include the presence of a defense system against superoxide based on manganese ions and a glutathione-dependent system for defense against nitric oxide which is under the control of a novel MerR-like transcriptional regulator. An understanding of the defenses against oxidative stress in N. gonorrhoeae and their regulation may provide new insights into the ways in which this bacterium survives challenges from polymorphonuclear leukocytes and urogenital epithelial cells.

Effect of manganese on grain refinement of Mg-Al based alloys

Manganese is a grain refiner for high purity Mg-3%Al, Mg-6%Al, Mg-9%Al, and commercial AZ31 (Mg-3%Al-1%Zn) alloys when introduced in the form of an Al-60%Mn master alloy splatter but the use of pure Mn flakes and ALTAB (TM) Mn75 tablets shows no grain refinement. Long time holding of the melt at 730 degrees C leads to an increase in grain size. The mechanism is attributed to the presence of all epsilon-AlMn phase (hexagonal close-packed) in the master alloy splatter. (c) 2006 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.

Interactions between iron, manganese, and the Al-Si eutectic in hypoeutectic Al-Si alloys

Sand-cast plates were used to determine the effect of iron and manganese concentrations on porosity levels in Al-9 pet Si-0.5 pet Mg alloys. Iron increased porosity levels. Manganese additions increased porosity levels in alloys with 0.1 pet Fe, but reduced porosity in alloys with 0.6 and I pet Fe. Thermal analysis and quenching were undertaken to determine the effect of iron and manganese on the solidification of the Al-Si eutectic. At high iron levels, the presence of large beta-Al5FeSi was found to reduce the number of eutectic nucleation events and increase the eutectic grain size. The preferential formation of alpha-Al15Mn3Si2 upon addition of manganese reversed these effects. It is proposed that this interaction is due to beta-Al5FeSi and the Al-Si eutectic having common nuclei. Porosity levels are proposed to be controlled by the eutectic grain size and the size of the iron-bearing intermetallic particles rather than the specific intermetallic phase that forms.

Phase equilibria in high MgO ferro- and silico-manganese smelting slags

Phase equilibria have been determined experimentally for pseudo-ternary sections of the form “MnO”- (CaO+MgO)-(SiO2+Al2O3) with a fixed Al2O3/SiO2 weight ratio of 0.17 and MgO/CaO weight ratios of 0.25 and 0.17 respectively for temperatures in the range 1473-1673 K. The primary phase fields present for the MgO/CaO weight ratio of 0.17 include manganosite (Mn,Mg,Ca)O; dicalcium silicate α-2(Ca,Mg,Mn)O·SiO2; merwinite 3CaO⋅(Mg,Mn)O⋅2SiO2; wollastonite [(Ca,Mg,Mn)O·SiO2]; diopside [(CaO,MgO,MnO,Al2O3)·SiO2]; tridymite (SiO2); tephroite [2(Mn,Mg)O·SiO2]; rhodonite [(Mn,Mg)O·SiO2] and melilite [2CaO·(MgO,MnO,Al2O3)·2(SiO2,Al2O3)]. For the section with MgO/CaO weight ratio of 0.25 the anorthite phase (CaO⋅Al2O3⋅2SiO2) is also present. The liquidus temperatures of ferro- and silico-manganese smelting slags have been determined. The liquidus temperatures at low MnO concentrations are shown to be principally dependent on the modified basicity weight ratio (CaO+MgO)/(SiO2+Al2O3).