Isolation and characterization of an Escherichia coli mutant with alteration in the outer membrane proteins of the cell envelope

1972 ◽  
Vol 290 ◽  
pp. 274-289 ◽  
Author(s):  
H.C. Wu
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Cell Envelope ◽  
Outer Membrane Proteins ◽  
Coli Mutant ◽  
Isolation And Characterization

Isolation and characterization of isogenic E. coli strains with alterations in the level of one or more major outer membrane proteins

1979 ◽  
Vol 25 (3) ◽  
pp. 423-427 ◽  
Author(s):  
John Foulds ◽  
Tuu-Jyi Chai
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
E Coli ◽  
Isolation And Characterization

Nearly isogenic Escherichia coli strains which carry mutations leading to altered levels of major outer membrane proteins have been prepared and genetically characterized.

scholarly journals Isolation and characterization of outer membrane proteins (OMPs) from Salmonella Gallinarum in chicken and antibiogram of the isolates

2016 ◽  
Vol 8 (4) ◽  
pp. 2292-2297
Author(s):  
Asma Ul Husna ◽  
Shabir Ahmad Mir ◽  
Rusheeba Manzoor ◽  
Farhat Pandit ◽  
Shakil Ahmad Wani ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Antimicrobial Agents ◽  
Outer Membrane Proteins ◽  
Specific Detection ◽  
Salmonella Gallinarum ◽  
Isolation And Characterization ◽  
Faecal Samples

Salmonella isolates should be distinguished as it may assist in tracing the source of an outbreak and monitoring trends in antimicrobial resistance associated with a particular type. The specific detection of these Salmonella serotypes is therefore extremely important in order to attribute an isolate to a previously known epidemic outbreak. The present investigation was to isolate and identify S. Gallinarum, to study variation in the profile of outer membrane proteins (OMPs) and to determine in vitro antibiogram of S. Gallinarum in poultry. A total of 228 faecal samples and 22 visceral samples suspected for Salmonellosis were collected, of these 15 samples (6.0%) were found positive for S. Gallinarum. In the present study, rfbS gene sequence was helpful in the serotype-specific detection of S. Gallinarum giving a 187 bp product. Salmonella Gallinarum crude protein extracts determined by SDSPAGE showed migration of OMPs as several bands at approximate moleculer weights of appx. 45 kDa, 55 kDa, 64 kDa, 65 kDa, 74 kDa, 110 kDa, 120 kDa, 135 kDa, 150 kDa,155 kDa, 200 kDa and above 200 kDa. The study indicated a definite variation in the profile of OMPs of various Salmonella Gallinarum strains with major OMPs in the range of appx 80-100 kDa which could be the target for vaccine production. All the isolates tested against 14 antimicrobial agents showed variable susceptibility pattern with highest resistance to nalidixic acid, ampicillin and sulphadiazine and sensitivity to chloramphenicol, gentamicin and enrofloxacin.

Isolation and characterization of outer membrane proteins of Edwardsiella tarda and its application in immunoassays

Aquaculture ◽  
2007 ◽  
Vol 272 (1-4) ◽  
pp. 98-104 ◽  
Author(s):  
Gokhlesh Kumar ◽  
Gaurav Rathore ◽  
U. Sengupta ◽  
V. Singh ◽  
D. Kapoor ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Edwardsiella Tarda ◽  
Isolation And Characterization

scholarly journals Helical Disposition of Proteins and Lipopolysaccharide in the Outer Membrane of Escherichia coli

2005 ◽  
Vol 187 (6) ◽  
pp. 1913-1922 ◽  
Author(s):  
Anindya S. Ghosh ◽  
Kevin D. Young
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Fluorescent Dyes ◽  
Cell Envelope ◽  
Outer Membrane Proteins ◽  
E Coli ◽  
Physiological Processes ◽  
Side Walls

ABSTRACT In bacteria, several physiological processes once thought to be the products of uniformly dispersed reactions are now known to be highly asymmetric, with some exhibiting interesting geometric localizations. In particular, the cell envelope of Escherichia coli displays a form of subcellular differentiation in which peptidoglycan and outer membrane proteins at the cell poles remain stable for generations while material in the lateral walls is diluted by growth and turnover. To determine if material in the side walls was organized in any way, we labeled outer membrane proteins with succinimidyl ester-linked fluorescent dyes and then grew the stained cells in the absence of dye. Labeled proteins were not evenly dispersed in the envelope but instead appeared as helical ribbons that wrapped around the outside of the cell. By staining the O8 surface antigen of E. coli 2443 with a fluorescent derivative of concanavalin A, we observed a similar helical organization for the lipopolysaccharide (LPS) component of the outer membrane. Fluorescence recovery after photobleaching indicated that some of the outer membrane proteins remained freely diffusible in the side walls and could also diffuse into polar domains. On the other hand, the LPS O antigen was virtually immobile. Thus, the outer membrane of E. coli has a defined in vivo organization in which a subfraction of proteins and LPS are embedded in stable domains at the poles and along one or more helical ribbons that span the length of this gram-negative rod.

scholarly journals Adhesion of Type 1-Fimbriated Escherichia coli to Abiotic Surfaces Leads to Altered Composition of Outer Membrane Proteins

2001 ◽  
Vol 183 (8) ◽  
pp. 2445-2453 ◽  
Author(s):  
Karen Otto ◽  
Joakim Norbeck ◽  
Thomas Larsson ◽  
Karl-Anders Karlsson ◽  
Malte Hermansson
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Cell Envelope ◽  
Outer Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Surface Characteristics ◽  
Abiotic Surfaces

ABSTRACT Phenotypic differences between planktonic bacteria and those attached to abiotic surfaces exist, but the mechanisms involved in the adhesion response of bacteria are not well understood. By the use of two-dimensional (2D) polyacrylamide gel electrophoresis, we have demonstrated that attachment of Escherichia coli to abiotic surfaces leads to alteration in the composition of outer membrane proteins. A major decrease in the abundance of resolved proteins was observed during adhesion of type 1-fimbriated E. colistrains, which was at least partly caused by proteolysis. Moreover, a study of fimbriated and nonfimbriated mutants revealed that these changes were due mainly to type 1 fimbria-mediated surface contact and that only a few changes occurred in the outer membranes of nonfimbriated mutant strains. Protein synthesis and proteolytic degradation were involved to different extents in adhesion of fimbriated and nonfimbriated cells. While protein synthesis appeared to affect adhesion of only the nonfimbriated strain, proteolytic activity mostly seemed to contribute to adhesion of the fimbriated strain. Using matrix-assisted laser desorption ionization–time of flight mass spectrometry, six of the proteins resolved by 2D analysis were identified as BtuB, EF-Tu, OmpA, OmpX, Slp, and TolC. While the first two proteins were unaffected by adhesion, the levels of the last four were moderately to strongly reduced. Based on the present results, it may be suggested that physical interactions between type 1 fimbriae and the surface are part of a surface-sensing mechanism in which protein turnover may contribute to the observed change in composition of outer membrane proteins. This change alters the surface characteristics of the cell envelope and may thus influence adhesion.

Bacteriocin 28b fromSerratia marcescensN28b: identification ofEscherichia colisurface components involved in bacteriocin binding and translocation

1996 ◽  
Vol 42 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Josefina Enfedaque ◽  
Santiago Ferrer ◽  
Joan Francesc Guasch ◽  
Miguel Regué ◽  
Joan Tomás
Keyword(s):  
Membrane Proteins ◽  
Serratia Marcescens ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Binding Ability ◽  
E Coli ◽  
The Core ◽  
Isolation And Characterization ◽  
Sensitivity Tests

Serratia marcescens N28b produces bacteriocin 28b, active against Escherichia coli. Bacteriocin sensitivity tests performed on a collection of E. coli envelope mutants, and isolation and characterization of E. coli bacteriocin-28b-insensitive mutants, showed that the core lipopolysaccharide, outer membrane proteins OmpA and OmpF, and TolQ, TolA, and TolB proteins are involved in bacteriocin 28b lethal activity. These mutants were assayed for bacteriocin 28b sensitivity under normal and bypass conditions, and their bacteriocin-binding ability was determined. The results obtained suggest that the core lipopolysaccaride and outer membrane proteins OmpA and OmpF are involved in bacteriocin 28b binding. Furthermore, bacteriocin 28b translocation requires proteins TolA, TolB, and TolQ.Key words: bacteriocin, receptors, translocation, Serratia marcescens.

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