Compilation of Escherichia coli K-12 outer membrane phage receptors – their function and some historical remarks

ABSTRACT Many Escherichia coli phages have been sequenced, but in most cases their sequences alone do not suffice to predict their host specificity. Analysis of phage resistant E. coli K-12 mutants have uncovered a certain set of outer membrane proteins and polysaccharides as receptors. In this review, a compilation of E. coli K12 phage receptors is provided and their functional characterization, often driven by studies on phage resistant mutants, is discussed in the historical context. While great progress has been made in this field thus far, several proteins in the outer membrane still await characterization as phage receptors.

Download Full-text

Influence of molecular size and osmolarity of sugars and dextrans on the synthesis of outer membrane proteins O-8 and O-9 of Escherichia coli K-12.

Journal of Bacteriology ◽

10.1128/jb.140.3.843-847.1979 ◽

1979 ◽

Vol 140 (3) ◽

pp. 843-847 ◽

Cited By ~ 116

Author(s):

H Kawaji ◽

T Mizuno ◽

S Mizushima

Keyword(s):

Escherichia Coli ◽

Membrane Proteins ◽

Outer Membrane ◽

Outer Membrane Proteins ◽

Molecular Size ◽

K 12

Download Full-text

BaeR participates in cephalosporins susceptibility by regulating the expression level of outer membrane proteins in Escherichia coli

The Journal of Biochemistry ◽

10.1093/jb/mvaa100 ◽

2020 ◽

Author(s):

Shuaiyang Wang ◽

Chunbo You ◽

Fareed Qumar Memon ◽

Geyin Zhang ◽

Yawei Sun ◽

...

Keyword(s):

Escherichia Coli ◽

Membrane Proteins ◽

Outer Membrane ◽

Efflux Pump ◽

Outer Membrane Proteins ◽

Expression Level ◽

Antibiotics Resistance ◽

Dilution Method ◽

Expression Levels ◽

E Coli

Abstract The two-component system BaeSR participates in antibiotics resistance of Escherichia coli. To know whether the outer membrane proteins involve in the antibiotics resistance mediated by BaeSR, deletion of acrB was constructed and the recombined plasmid p-baeR was introduced into E. coli K12 and K12△acrB. Minimum inhibitory concentrations (MICs) of antibacterial agents were determined by 2-fold broth micro-dilution method. Gene expressions related with major outer membrane proteins and multidrug efflux pump-related genes were determined by real-time quantitative reverse transcription polymerase chain reaction. The results revealed that the MICs of K12ΔacrB to the tested drugs except for gentamycin and amikacin decreased 2- to 16.75-folds compared with those of K12. When BaeR was overexpressed, the MICs of K12ΔacrB/p-baeR to ceftiofur and cefotaxime increased 2.5- and 2-fold, respectively, compared with their corresponding that of K12△acrB. At the same time, the expression levels of ompC, ompF, ompW, ompA and ompX showed significant reduction in K12ΔacrB/p-baeR as compared with K12△acrB. Moreover, the expression levels of ompR, marA, rob and tolC also significantly ‘decreased’ in K12ΔacrB/p-baeR. These findings indicated that BaeR overproduction can decrease cephalosporins susceptibility in acrB-free E. coli by decreasing the expression level of outer membrane proteins.

Download Full-text

Ib-M6 Antimicrobial Peptide: Antibacterial Activity against Clinical Isolates of Escherichia coli and Molecular Docking

Antibiotics ◽

10.3390/antibiotics9020079 ◽

2020 ◽

Vol 9 (2) ◽

pp. 79 ◽

Cited By ~ 1

Author(s):

J. M. Flórez-Castillo ◽

P. Rondón-Villareal ◽

J. L. Ropero-Vega ◽

S. Y. Mendoza-Espinel ◽

J. A. Moreno-Amézquita ◽

...

Keyword(s):

Escherichia Coli ◽

Antibacterial Activity ◽

Molecular Docking ◽

Outer Membrane ◽

Docking Simulations ◽

E Coli ◽

Pathogenic Escherichia Coli ◽

Membrane Components ◽

K 12 ◽

Susceptibility Assay

The Ib-M6 peptide has antibacterial activity against non-pathogenic Escherichia coli K-12 strain. The first part of this study determines the antibacterial activity of Ib-M6 against fourteen pathogenic strains of E. coli O157:H7. Susceptibility assay showed that Ib-M6 had values of Minimum Inhibitory Concentration (MIC) lower than streptomycin, used as a reference antibiotic. Moreover, to predict the possible interaction between Ib-M6 and outer membrane components of E. coli, we used molecular docking simulations where FhuA protein and its complex with Lipopolysaccharide (LPS–FhuA) were used as targets of the peptide. FhuA/Ib-M6 complexes had energy values between −39.5 and −40.5 Rosetta Energy Units (REU) and only one hydrogen bond. In contrast, complexes between LPS–FhuA and Ib-M6 displayed energy values between −25.6 and −40.6 REU, and the presence of five possible hydrogen bonds. Hence, the antimicrobial activity of Ib-M6 peptide shown in the experimental assays could be caused by its interaction with the outer membrane of E. coli.

Download Full-text

The c-Type Cytochrome OmcA Localizes to the Outer Membrane upon Heterologous Expression in Escherichia coli

Journal of Bacteriology ◽

10.1128/jb.00395-08 ◽

2008 ◽

Vol 190 (14) ◽

pp. 5127-5131 ◽

Cited By ~ 18

Author(s):

James W. Donald ◽

Matthew G. Hicks ◽

David J. Richardson ◽

Tracy Palmer

Keyword(s):

Escherichia Coli ◽

Outer Membrane ◽

Shewanella Oneidensis ◽

Type Ii Secretion ◽

Type Ii ◽

E Coli ◽

Expression In Escherichia Coli ◽

Type Ii Secretion System ◽

Surface Localization ◽

K 12

ABSTRACT We have functionally produced the outer membrane cytochrome OmcA from Shewanella oneidensis in Escherichia coli. Substrate accessibility experiments indicate that OmcA is surface exposed in an E. coli B strain but not in a K-12 strain. We show that a functional type II secretion system is required for surface localization.

Download Full-text

A Peptidomimetic Antibiotic Targets Outer Membrane Proteins and Disrupts Selectively the Outer Membrane in Escherichia coli

Journal of Biological Chemistry ◽

10.1074/jbc.m115.691725 ◽

2015 ◽

Vol 291 (4) ◽

pp. 1921-1932 ◽

Cited By ~ 47

Author(s):

Matthias Urfer ◽

Jasmina Bogdanovic ◽

Fabio Lo Monte ◽

Kerstin Moehle ◽

Katja Zerbe ◽

...

Keyword(s):

Escherichia Coli ◽

Outer Membrane ◽

Outer Membrane Proteins ◽

Permeability Barrier ◽

Gram Negative ◽

Fluorescence Studies ◽

E Coli ◽

Interaction Sites ◽

External Stresses ◽

Antibiotic Discovery

Increasing antibacterial resistance presents a major challenge in antibiotic discovery. One attractive target in Gram-negative bacteria is the unique asymmetric outer membrane (OM), which acts as a permeability barrier that protects the cell from external stresses, such as the presence of antibiotics. We describe a novel β-hairpin macrocyclic peptide JB-95 with potent antimicrobial activity against Escherichia coli. This peptide exhibits no cellular lytic activity, but electron microscopy and fluorescence studies reveal an ability to selectively disrupt the OM but not the inner membrane of E. coli. The selective targeting of the OM probably occurs through interactions of JB-95 with selected β-barrel OM proteins, including BamA and LptD as shown by photolabeling experiments. Membrane proteomic studies reveal rapid depletion of many β-barrel OM proteins from JB-95-treated E. coli, consistent with induction of a membrane stress response and/or direct inhibition of the Bam folding machine. The results suggest that lethal disruption of the OM by JB-95 occurs through a novel mechanism of action at key interaction sites within clusters of β-barrel proteins in the OM. These findings open new avenues for developing antibiotics that specifically target β-barrel proteins and the integrity of the Gram-negative OM.

Download Full-text

Localized adherence by enteropathogenic Escherichia coli is an inducible phenotype associated with the expression of new outer membrane proteins.

Journal of Experimental Medicine ◽

10.1084/jem.174.5.1167 ◽

1991 ◽

Vol 174 (5) ◽

pp. 1167-1177 ◽

Cited By ~ 64

Author(s):

J Vuopio-Varkila ◽

G K Schoolnik

Keyword(s):

Escherichia Coli ◽

Membrane Proteins ◽

Outer Membrane ◽

De Novo ◽

Outer Membrane Proteins ◽

Temporal Correlation ◽

Enteropathogenic Escherichia Coli ◽

E Coli

Enteropathogenic Escherichia coli grow as discrete colonies on the mucous membranes of the small intestine. A similar pattern can be demonstrated in vitro; termed localized adherence (LA), it is characterized by the presence of circumscribed clusters of bacteria attached to the surfaces of cultured epithelial cells. The LA phenotype was studied using B171, an O111:NM enteropathogenic E. coli (EPEC) strain, and HEp-2 cell monolayers. LA could be detected 30-60 min after exposure of HEp-2 cells to B171. However, bacteria transferred from infected HEp-2 cells to fresh monolayers exhibited LA within 15 min, indicating that LA is an inducible phenotype. Induction of the LA phenotype was found to be associated with de novo protein synthesis and changes in the outer membrane proteins, including the production of a new 18.5-kD polypeptide. A partial NH2-terminal amino acid sequence of this polypeptide was obtained and showed it to be identical through residue 12 to the recently described bundle-forming pilus subunit of EPEC. Expression of the 18.5-kD polypeptide required the 57-megadalton enteropathogenic E. coli adherence plasmid previously shown to be required for the LA phenotype in vitro and full virulence in vivo. This observation, the correspondence of the 18.5-kD polypeptide to an EPEC-specific pilus protein, and the temporal correlation of its expression with the development of the LA phenotype suggest that it may contribute to the EPEC colonial mode of growth.

Download Full-text