Toxicity of Cadmium and Copper in Chlamydomonas reinhardtii Wild-Type (WT 2137) and Cell Wall Deficient Mutant Strain (CW 15)

1998 ◽  
Vol 60 (2) ◽  
pp. 306-311 ◽  
Author(s):  
M. N. V. Prasad ◽  
K. Drej ◽  
A. Skawi &#96 ska ◽  
K. Stra &#94 ka
Keyword(s):  
Cell Wall ◽  
Chlamydomonas Reinhardtii ◽  
Mutant Strain ◽  
Deficient Mutant ◽  
Wild Type

Cell-wall abnormalities of a Chlamydomonas reinhardtii mutant strain under suboptimal growth conditions

Planta ◽  
1991 ◽  
Vol 183 (1) ◽  
Author(s):  
J�rgen Voigt ◽  
Dieter Mergenhagen ◽  
Irmhild Wachholz ◽  
Elsbeth Manshard ◽  
Marianne Mix
Keyword(s):  
Cell Wall ◽  
Chlamydomonas Reinhardtii ◽  
Mutant Strain ◽  
Growth Conditions

scholarly journals A New Transformation-Deficient Mutant ofHaemophilus influenzae Rd with Normal DNA Uptake

1998 ◽  
Vol 180 (3) ◽  
pp. 746-748 ◽  
Author(s):  
M. L. Gwinn ◽  
R. Ramanathan ◽  
H. O. Smith ◽  
J.-F. Tomb
Keyword(s):  
Haemophilus Influenzae ◽  
Mutant Strain ◽  
Competence Development ◽  
Transformation Frequency ◽  
Dna Uptake ◽  
Deficient Mutant ◽  
Wild Type ◽  
Gram Negative ◽  
Ofhaemophilus Influenzae

ABSTRACT Haemophilus influenzae Rd is a gram-negative natural transformer. A mutant strain, RJ248, that has normal DNA uptake and translocation but whose transformation frequency is 300 times lower than that of wild-type H. influenzae and whose phage recombination is 8 times lower was isolated. The affected gene,comM, is induced during competence development in wild-typeH. influenzae but not in RJ248.

scholarly journals Mycobacterium smegmatis d-Alanine Racemase Mutants Are Not Dependent on d-Alanine for Growth

2002 ◽  
Vol 46 (1) ◽  
pp. 47-54 ◽  
Author(s):  
Ofelia Chacon ◽  
Zhengyu Feng ◽  
N. Beth Harris ◽  
Nancy E. Cáceres ◽  
L. Garry Adams ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mutant Strain ◽  
Mycobacterium Smegmatis ◽  
Type Strain ◽  
Wild Type Strain ◽  
Kanamycin Resistance ◽  
Alanine Racemase ◽  
Wild Type ◽  
Peptidoglycan Biosynthesis ◽  
Insertional Inactivation

ABSTRACT Mycobacterium smegmatis is a fast-growing nonpathogenic species particularly useful in studying basic cellular processes of relevance to pathogenic mycobacteria. This study focused on the d-alanine racemase gene (alrA), which is involved in the synthesis of d-alanine, a basic component of peptidoglycan that forms the backbone of the cell wall. M. smegmatis alrA null mutants were generated by homologous recombination using a kanamycin resistance marker for insertional inactivation. Mutants were selected on Middlebrook medium supplemented with 50 mM d-alanine and 20 μg of kanamycin per ml. These mutants were also able to grow in standard and minimal media without d-alanine, giving rise to colonies with a drier appearance and more-raised borders than the wild-type strain. The viability of the mutants and independence of d-alanine for growth indicate that inactivation of alrA does not impose an auxotrophic requirement for d-alanine, suggesting the existence of a new pathway of d-alanine biosynthesis in M. smegmatis. Biochemical analysis demonstrated the absence of any detectable d-alanine racemase activity in the mutant strains. In addition, the alrA mutants displayed hypersusceptibility to the antimycobacterial agent d-cycloserine. The MIC of d-cycloserine for the mutant strain was 2.56 μg/ml, 30-fold less than that for the wild-type strain. Furthermore, this hypersusceptibility was confirmed by the bactericidal action of d-cycloserine on broth cultures. The kinetic of killing for the mutant strain followed the same pattern as that for the wild-type strain, but at a 30-fold-lower drug concentration. This effect does not involve a change in the permeability of the cell wall by this drug and is consistent with the identification of d-alanine racemase as a target of d-cycloserine. This outcome is of importance for the design of novel antituberculosis drugs targeting peptidoglycan biosynthesis in mycobacteria.

Genetic analysis of developmental mechanisms in hydra. XIX. Stimulation of regeneration by injury in the regeneration-deficient mutant strain, reg-16

Development ◽  
1989 ◽  
Vol 105 (3) ◽  
pp. 521-528
Author(s):  
E. Kobatake ◽  
T. Sugiyama
Keyword(s):  
Mutant Strain ◽  
Deficient Mutant ◽  
Wild Type ◽  
Regenerative Capacity ◽  
Activation Level ◽  
Original Number ◽  
Morphogenetic Potential ◽  
Hydra Magnipapillata ◽  
Strain Mechanisms ◽  
Stimulation Of

A mutant strain of Hydra magnipapillata, reg-16, has a very low regenerative capacity. After head removal, it usually restores 10–20% of the original number of tentacles in 7 days. A procedure was found to markedly improve tentacle regeneration in this strain. The closed wound located at the apical regenerating tip of the decapitated polyp was gently reopened using a pair of forceps. Reg-16 polyps treated in this way at 24 and 48 h after head removal restored nearly all of the original number of tentacles in 7 days. A lateral tissue transplantation procedure was employed to examine the effect of wound reopening on the morphogenetic potential of decapitated reg-16 polyps. Wound reopening produced a significant increase in head activation level without producing a preceding decrease in head inhibition level. This and other observations suggest that the coupled activation-inhibition changes that normally occur after head removal from the wild-type hydra do not occur in this strain. Mechanisms responsible for the wound reopening effect and the absence of activation-inhibition coupling in the mutant strain reg-16 are discussed.

scholarly journals In Vitro Characterization of the Microglial Inflammatory Response to Streptococcus suis, an Important Emerging Zoonotic Agent of Meningitis

2010 ◽  
Vol 78 (12) ◽  
pp. 5074-5085 ◽  
Author(s):  
María de la Cruz Domínguez-Punaro ◽  
Mariela Segura ◽  
Irazú Contreras ◽  
Claude Lachance ◽  
Mathieu Houde ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Cell Wall ◽  
Protein Kinase ◽  
Inflammatory Response ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Microglial Cells ◽  
Deficient Mutant ◽  
Wild Type ◽  
The Brain

ABSTRACT Streptococcus suis is an important swine and human pathogen responsible for septicemia and meningitis. In vivo research in mice suggested that in the brain, microglia might be involved in activating the inflammatory response against S. suis. The aim of this study was to better understand the interactions between S. suis and microglia. Murine microglial cells were infected with a virulent wild-type strain of S. suis. Two isogenic mutants deficient at either capsular polysaccharide (CPS) or hemolysin production were also included. CPS contributed to S. suis resistance to phagocytosis and regulated the inflammatory response by hiding proinflammatory components from the bacterial cell wall, while the absence of hemolysin, a potential cytotoxic factor, did not have a major impact on S. suis interactions with microglia. Wild-type S. suis induced enhanced expression of Toll-like receptor 2 by microglial cells, as well as phophotyrosine, protein kinase C, and different mitogen-activated protein kinase signaling events. However, cells infected with the CPS-deficient mutant showed overall stronger and more sustained phosphorylation profiles. CPS also modulated inducible nitric oxide synthase expression and further nitric oxide production from S. suis-infected microglia. Finally, S. suis-induced NF-κB translocation was faster for cells stimulated with the CPS-deficient mutant, suggesting that bacterial cell wall components are potent inducers of NF-κB. These results contribute to increase the knowledge of mechanisms underlying S. suis inflammation in the brain and will be useful in designing more efficient anti-inflammatory strategies for meningitis.

scholarly journals Role of Porphyromonas gingivalis FeoB2 in Metal Uptake and Oxidative Stress Protection

2006 ◽  
Vol 74 (7) ◽  
pp. 4214-4223 ◽  
Author(s):  
Jia He ◽  
Hiroshi Miyazaki ◽  
Cecilia Anaya ◽  
Fan Yu ◽  
W. Andrew Yeudall ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Mutant Strain ◽  
Parental Strain ◽  
Atmospheric Oxygen ◽  
Host Cells ◽  
Deficient Mutant ◽  
Wild Type ◽  
Stress Protection ◽  
Oxidative Stress Protection

ABSTRACT Porphyromonas gingivalis, a gram-negative anaerobic bacterium, is a recognized periodontopathogen. It exhibits a high degree of aerotolerance and is able to survive in host cells, indicating that efficient oxidative stress protection mechanisms must be present in this organism. Manganese homeostasis plays a major role in oxidative stress protection in a variety of organisms; however, the transport and role of this metal in P. gingivalis is not well understood. Analysis of the genome of P. gingivalis W83 revealed the presence of two genes encoding homologs of a ferrous iron transport protein, FeoB1 and FeoB2. FeoB2 has been implicated in manganese accumulation in P. gingivalis. We sought to determine the role of the FeoB2 protein in metal transport as well as its contribution to resistance to oxygen radicals. Quantitative reverse transcriptase PCR analyses demonstrated that expression of feoB2 is induced in the presence of oxygen. The role of FeoB2 was investigated using an isogenic mutant strain deficient in the putative transporter. We characterized the FeoB2-mediated metal transport using 55Fe2+ and 54Mn2+. The FeoB2-deficient mutant had dramatically reduced rates of manganese uptake (0.028 pmol/min/107 bacteria) compared with the parental strain (0.33 pmol/min/107 bacteria) (after 20 min of uptake using 50 nM of 54Mn2+). The iron uptake rates, however, were higher in the mutant strain (0.75 pmol/min/107 bacteria) than in the wild type (0.39 pmol/min/107 bacteria). Interestingly, reduced survival rates were also noted for the mutant strain after exposure to H2O2 and to atmospheric oxygen compared to the parental strain cultured under the same conditions. In addition, in vitro infection of host cells with the wild type, the FeoB2-deficient mutant, and the same-site revertant revealed that the mutant had a significantly decreased capability for intracellular survival in the host cells compared to the wild-type strain. Our results demonstrate that feoB2 encodes a major manganese transporter required for protection of the bacterium from oxidative stress generated by atmospheric oxygen and H2O2. Furthermore, we show that FeoB2 and acquisition of manganese are required for intracellular survival of P. gingivalis in host cells.

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