scholarly journals ANTI-Escherichia coli NON-PATHOGENIC STRAIN ACTIVITY OF COMPLEX COMPOUND BASED ON COPPER(II) AND 2,4,5- TRIPHENYL-1H-IMIDAZOLE

2021 ◽  
Vol 14 (02) ◽  
pp. 672-675
Author(s):  
T. H. Sucipto ◽  
W. Setyarini ◽  
F. Martak ◽  
D. Raharjo
2018 ◽  
Vol 16 (1) ◽  
pp. 59 ◽  
Author(s):  
Masruri Masruri ◽  
Rekfa Wika Amini ◽  
Mohammad Farid Rahman

Catalytic oxidation of alpha-pinene was investigated using potassium permanganate as an oxidant. The reaction consumed catalyst following stoichiometric amount instead of the catalytic one. The keto-carboxylate compound 2 was afforded as the oxidation product. Further study of its complex compound with copper(II) and zinc(II) was also reported including their activity for inhibiting the growth of Staphylococcus aureus and Escherichia coli. In overall, the complex compound shows important result by inhibiting the bacterial growth.


2015 ◽  
Vol 34 (4) ◽  
Author(s):  
P. R. Bachanti ◽  
Shilpa Vij

The sodium caseinate fermentated by <italic>Lactobacillus fermentum</italic> NCDC 141 showed antimicrobial activity against pathogenic strain <italic>Escherichia coli</italic> O157:H7 and against some spoilage causing microbial species <italic>Bacillus subtilis</italic> NCDC 70, <italic>Saccharomyces cerevisiae</italic> NCDC 47 and <italic>Rhizopus oryzae</italic> NCDC 52 .This property of <italic>Lactobacillus fermentum</italic> NCDC 141 may have bioprotective applicability in milk based formula, which needs further exploration to confirm its potentility.


Microbiology ◽  
2011 ◽  
Vol 157 (3) ◽  
pp. 774-785 ◽  
Author(s):  
Jérôme Tourret ◽  
Meryem Aloulou ◽  
Louis Garry ◽  
Olivier Tenaillon ◽  
Sara Dion ◽  
...  

Finding two or more genotypes of a single species within an infected sample is a not infrequent event. In this work, three Escherichia coli strains of decreasing extra-intestinal virulence (pathogenic B2S and B1S strains, and the avirulent K-12 MG1655 strain) were tested in septicaemia and urinary tract infection (UTI) mouse models, either separately or in pairs. Survival was monitored and bacteria were counted in various organs. Serum interleukin (IL)-6, tumour necrosis factor alpha (TNFα) and IL-10 were measured. We show that a mix of high amounts of B1S or of MG1655 with low amounts of B2S killed more rapidly (B1S), or killed more mice (MG1655), than either high amounts of B1S, high amounts of MG1655 or low amounts of B2S separately in the mouse septicaemia model. This bacterial synergy persisted when high amounts of dead or abnormal-LPS K-12 cells were injected together with a low amount of B2S. In both septicaemia and UTI models, significantly more bacteria were recovered from the organs of mice injected with the MG1655/B2S mix than from those of mice injected with the inocula separately. Consistently, in the septicaemia model, more IL-6 was secreted before death by the mice that were injected with the mix of bacteria than by the mice that were injected with the inocula separately. The synergistically enhanced mortality in the case of co-infection in the septicaemia model persisted in RFcγ −/−, Myd88 −/− and IL-6−/− knockout mice. This synergistically increased virulence resulting from the interaction between an avirulent and a pathogenic strain of the same bacterial species raises questions about the role of avirulent bacteria in the development of some extra-intestinal infections.


Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).


Author(s):  
Manfred E. Bayer

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.


Author(s):  
Manfred E. Bayer

The first step in the infection of a bacterium by a virus consists of a collision between cell and bacteriophage. The presence of virus-specific receptors on the cell surface will trigger a number of events leading eventually to release of the phage nucleic acid. The execution of the various "steps" in the infection process varies from one virus-type to the other, depending on the anatomy of the virus. Small viruses like ØX 174 and MS2 adsorb directly with their capsid to the bacterial receptors, while other phages possess attachment organelles of varying complexity. In bacteriophages T3 (Fig. 1) and T7 the small conical processes of their heads point toward the adsorption site; a welldefined baseplate is attached to the head of P22; heads without baseplates are not infective.


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