ВЫДЕЛЕНИЕ БАКТЕРИОФАГОВ ПРОТИВ ВОЗБУДИТЕЛЯ МЫТА ЛОШАДЕЙ - STREPTOCOCCUS EQUI И ИЗУЧЕНИЕ ИХ БИОЛОГИЧЕСКИХ СВОЙСТВ

Habarshy ◽  
2021 ◽  
pp. 17-26
Author(s):  
Б.А. Еспембетов ◽  
Е.А. Булатов ◽  
М.К. Сармыкова ◽  
Е.Б. Серікбай ◽  
А.А. Самбетбаев
Keyword(s):  
Escherichia Coli ◽  
Streptococcus Equi

Изучение биологических свойств мытного фага - это важный этап при создании биопрепаратов, фагоиндикации и идентификации бактерий. Главным признаком воздействия фага на чувствительной бактерии является их лизис, сопровождающийся выходом в среду новых вирионов фага.Целью исследований является получение бактериофага для терапии мыта лошадей.Новизной данной работы является то, что впервые в Казахстане проводятся иссле-дования по изучению биологических свойств бактериофагов для терапии мыта лошадей, выделенных объектов внешней среды и биоматериала из хозяйств Алматинской области. Объектами исследования служили бактериофаги, выделенные из образцов внешней среды, всего исследовано 19 проб. Для изучения биологических свойств в качестве индикаторных тест-культур были использована штамм Str.equi. Все изучаемые фаги имели титр 107-109 по Аппельману и 109-1010 по Грациа, обладали выраженной специфичностью в отношении к Streptococcus equi и не проявляли активности в отношении Streptococcus aureus и Escherichia coli, они сохраняли литическую активность в течение 2 месяцев, были устойчивы к нагреванию в пределах 60°С - 95°С в течение 30 мин. Фаги были устойчивы к действию 10% раствора хлороформа в течение 45 мин.

scholarly journals Immunogenicity of Escherichia coli Expressing Streptococcus equi subsp. equi Recombinant SeM

2021 ◽  
Vol 64 ◽  
Author(s):  
Matheus Costa da Rosa ◽  
Neida Lucia Conrad ◽  
Carina Martins Moraes ◽  
Leandro do Monte Ribas ◽  
Carlos Eduardo Wayne Nogueira ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Streptococcus Equi

scholarly journals Isolamento e teste de susceptibilidade a antimicrobianos de bactérias em infecções uterinas de éguas

1999 ◽  
Vol 51 (3) ◽  
pp. 213-216 ◽  
Author(s):  
N. Silva ◽  
C.E. Braga ◽  
G.M. Costa ◽  
F.C.F. Lobato
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Proteus Mirabilis ◽  
Rhodococcus Equi ◽  
Minas Gerais ◽  
Streptococcus Equi ◽  
Bacillus Spp

Foram examinados 206 "swabs" cervicais e uterinos de éguas de várias raças, de diversas regiões do Estado de Minas Gerais, durante o período de 1986 a 1996. Cerca de 164 "swabs" foram positivos para a presença de microrganismos causadores de endometrites. Streptococcus equi subsp. zooepidemicus (25,7%) e Escherichia coli (15,1%) foram os principais agentes infecciosos isolados. Outros microrganismos presentes foram: Staphylococcus aureus (9,2%), Streptococcus alfa-hemolítico (9,2%), Pseudomonas aeruginosa (3,9%), Staphylococcus coagulase negativo (6,3%), Bacillus spp. (1,9%), Rhodococcus equi (3,4%) e Proteus mirabilis (1,5%). As provas de susceptibilidade aos antimicrobianos revelaram que amicacina e gentamicina (70,2%), ampicilina (59,5%) e cloranfenicol (59,5%) foram os antibióticos de maior ação in vitro contra os microrganismos isolados.

scholarly journals Cloning, Expression, Sequence Analysis, and Characterization of Streptokinases Secreted by Porcine and Equine Isolates of Streptococcus equisimilis

1999 ◽  
Vol 67 (12) ◽  
pp. 6478-6486 ◽  
Author(s):  
Armando R. Caballero ◽  
Richard Lottenberg ◽  
Kenneth H. Johnston
Keyword(s):  
Escherichia Coli ◽  
Sequence Analysis ◽  
Phase Analysis ◽  
Fluid Phase ◽  
Plasminogen Activators ◽  
Plasminogen Activation ◽  
Streptococcus Equi

ABSTRACT Streptokinases secreted by nonhuman isolates of group C streptococci (Streptococcus equi, S. equisimilis, and S. zooepidemicus) have been shown to bind to different mammalian plasminogens but exhibit preferential plasminogen activity. The streptokinase genes from S. equisimilis strains which activated either equine or porcine plasminogen were cloned, sequenced, and expressed in Escherichia coli. The streptokinase secreted by the equine isolate had little similarity to any known streptokinases secreted by either human or porcine isolates. The streptokinase secreted by the porcine isolate had limited structural and functional similarities to streptokinases secreted by human isolates. Plasminogen activation studies with immobilized (His)6-tagged recombinant streptokinases indicated that these recombinant streptokinases interacted with plasminogen in a manner similar to that observed when streptokinase and plasminogen interact in the fluid phase. Analysis of the cleavage products of the streptokinase-plasminogen interaction indicated that human, equine, and porcine plasminogens were all cleaved at the same highly conserved site. The site at which streptokinase was cleaved to form altered streptokinase (Sk*) was also determined. This study confirmed not only the presence of streptokinases in nonhuman S. equisimilis isolates but also that these proteins belong to a family of plasminogen activators more diverse than previously thought.

Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 166-167 ◽  
Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Spatial Arrangement ◽  
Small Subunit ◽  
Antibody Binding ◽  
Immuno Electron Microscopy

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).

Sites of Adsorption of the Bacteriophages T3 and T5 on the Wall of Escherichia Coli B.

1967 ◽  
Vol 25 ◽  
pp. 96-97
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Electron Microscope ◽  
Uranyl Acetate ◽  
E Coli ◽  
Receptor Sites ◽  
Rigid Cell Wall ◽  
Host Cell Surface ◽  
Bacterial Viruses ◽  
Escherichia Coli B

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.

Infection of Escherichia coli with bacteriophages

1969 ◽  
Vol 27 ◽  
pp. 370-371
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Nucleic Acid ◽  
Cell Surface ◽  
Virus Type ◽  
Infection Process ◽  
Adsorption Site ◽  
The Other ◽  
Specific Receptors ◽  
Bacterial Receptors

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.

The Nature of the Intramembrane Particle

1980 ◽  
Vol 38 ◽  
pp. 688-691
Author(s):  
A.J. Verkleij
Keyword(s):  
Escherichia Coli ◽  
Tight Junction ◽  
Gap Junction ◽  
The Other ◽  
Fracture Face ◽  
Band 3 Protein ◽  
Satisfactory Explanation ◽  
Freeze Fracturing ◽  
Intramembrane Particle ◽  
Luminal Membrane

Freeze-fracturing splits membranes into two helves, thus allowing an examination of the membrane interior. The 5-10 rm particles visible on both monolayers are widely assumed to be proteinaceous in nature. Most membranes do not reveal impressions complementary to particles on the opposite fracture face, if the membranes are fractured under conditions without etching. Even if it is considered that shadowing, contamination or fracturing itself might obscure complementary pits', there is no satisfactory explanation why under similar physical circimstances matching halves of other membranes can be visualized. A prominent example of uncomplementarity is found in the erythrocyte manbrane. It is wall established that band 3 protein and possibly glycophorin represents these nonccmplanentary particles. On the other hand a number of membrane types show pits opposite the particles. Scme well known examples are the ";gap junction',"; tight junction, the luminal membrane of the bladder epithelial cells and the outer membrane of Escherichia coli.

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