scholarly journals Correction to Structural Characterization of a Model Gram-Negative Bacterial Surface Using Lipopolysaccharides from Rough Strains of Escherichia coli

2014 ◽  
Vol 15 (8) ◽  
pp. 3213-3213
Author(s):  
Anton P. Le Brun ◽  
Luke A. Clifton ◽  
Candice E. Halbert ◽  
Binhua Lin ◽  
Mati Meron ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Characterization ◽  
Gram Negative ◽  
Bacterial Surface

scholarly journals Structural Characterization of a Model Gram-Negative Bacterial Surface Using Lipopolysaccharides from Rough Strains of Escherichia coli

2013 ◽  
Vol 14 (6) ◽  
pp. 2014-2022 ◽  
Author(s):  
Anton P. Le Brun ◽  
Luke A. Clifton ◽  
Candice E. Halbert ◽  
Binhua Lin ◽  
Mati Meron ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Characterization ◽  
Gram Negative ◽  
Bacterial Surface

Biochemical and Structural Characterization of an Unusual Group of Gram-negative, Anaerobic Rods from Human Periapical Osteitis

Microbiology ◽  
1986 ◽  
Vol 132 (2) ◽  
pp. 417-426
Author(s):  
M. Haapasalo ◽  
H. Ranta ◽  
H. Shah ◽  
K. Ranta ◽  
K. Lounatmaa ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Gram Negative

scholarly journals Characterization of the 6'-N-aminoglycoside acetyltransferase gene aac(6')-Im [corrected] associated with a sulI-type integron.

1997 ◽  
Vol 41 (2) ◽  
pp. 314-318 ◽  
Author(s):  
E Hannecart-Pokorni ◽  
F Depuydt ◽  
L de wit ◽  
E van Bossuyt ◽  
J Content ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Amino Acid ◽  
Resistance Gene ◽  
Citrobacter Freundii ◽  
Gram Negative ◽  
Gene Environment ◽  
Insert Region ◽  
Klebsiella Spp

The amikacin resistance gene aac(6')-Im [corrected] from Citrobacter freundii Cf155 encoding an aminoglycoside 6'-N-acetyltransferase was characterized. The gene was identified as a coding sequence of 521 bp located down-stream from the 5' conserved segment of an integron. The sequence of this aac(6')-Im [corrected] gene corresponded to a protein of 173 amino acids which possessed 64.2% identity in a 165-amino-acid overlap with the aac(6')-Ia gene product (F.C. Tenover, D. Filpula, K.L. Phillips, and J. J. Plorde, J. Bacteriol. 170:471-473, 1988). By using PCR, the aac(6')-Im [corrected] gene could be detected in 8 of 86 gram-negative clinical isolates from two Belgian hospitals, including isolates of Citrobacter, Klebsiella spp., and Escherichia coli. PCR mapping of the aac(6')-Im [corrected] gene environment in these isolates indicated that the gene was located within a sulI-type integron; the insert region is 1,700 bases long and includes two genes cassettes, the second being ant (3")-Ib.

scholarly journals A Novel Method of Serum Resistance by Escherichia coli That Causes Urosepsis

mBio ◽  
2018 ◽  
Vol 9 (3) ◽  
Author(s):  
Carrie F. Coggon ◽  
Andrew Jiang ◽  
Kelvin G. K. Goh ◽  
Ian R. Henderson ◽  
Mark A. Schembri ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Urinary Tract ◽  
Serum Resistance ◽  
Gram Negative ◽  
Content Type ◽  
Bacterial Surface ◽  
O Antigen ◽  
High Prevalence ◽  
Novel Method ◽  
Inhibitory Antibodies

ABSTRACT Uropathogenic Escherichia coli (UPEC) is the most common cause of urinary tract infection, which in some patients can develop into life-threatening urosepsis. Serum resistance is a key virulence trait of strains that cause urosepsis. Recently, we identified a novel method of serum resistance in patients with Pseudomonas aeruginosa lung infections, where patients possessed antibodies that inhibited complement-mediated killing (instead of protecting against infection). These inhibitory antibodies were of the IgG2 subtype, specific to the O-antigen component of lipopolysaccharide (LPS) and coated the bacterial surface, preventing bacterial lysis by complement. As this mechanism could apply to any Gram-negative bacterial infection, we hypothesized that inhibitory antibodies may represent an uncharacterized mechanism of serum resistance in UPEC. To test this, 45 urosepsis patients with paired blood culture UPEC isolates were screened for serum titers of IgG2 specific for their cognate strain’s LPS. Eleven patients had sufficiently high titers of the antibody to inhibit serum-mediated killing of UPEC isolates by pooled healthy control sera. Depletion of IgG or removal of O-antigen restored sensitivity of the isolates to the cognate patient serum. Importantly, the isolates from these 11 patients were more sensitive to killing by serum than isolates from patients with no inhibitory antibodies. This suggests the presence of inhibitory antibodies may have allowed these strains to infect the bloodstream. The high prevalence of patients with inhibitory antibodies (24%) suggests that this phenomenon is an important mechanism of UPEC serum resistance. LPS-specific inhibitory antibodies have now been identified against three Gram-negative pathogens that cause disparate diseases. IMPORTANCE Despite improvements in the early detection and management of sepsis, morbidity and mortality are still high. Infections of the urinary tract are one of the most frequent sources of sepsis with Escherichia coli the main causative agent. Serum resistance is vital for bacteria to infect the bloodstream. Here we report a novel method of serum resistance found in patients with UPEC-mediated sepsis. Antibodies in sera usually protect against infection, but here we found that 24% of patients expressed “inhibitory antibodies” capable of preventing serum-mediated killing of their infecting isolate. Our data suggest that these antibodies would allow otherwise serum-sensitive UPEC strains to cause sepsis. The high prevalence of patients with inhibitory antibodies in this cohort suggests that this is a widespread mechanism of resistance to complement-mediated killing in urosepsis patients, invoking the potential for the application of new methods to prevent and treat sepsis.

Iron–sulfur repair YtfE protein from Escherichia coli: structural characterization of the di-iron center

2008 ◽  
Vol 13 (5) ◽  
pp. 765-770 ◽  
Author(s):  
Smilja Todorovic ◽  
Marta C. Justino ◽  
Gerd Wellenreuther ◽  
Peter Hildebrandt ◽  
Daniel H. Murgida ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Characterization ◽  
Iron Sulfur ◽  
Iron Center

scholarly journals Characterization of the β-lactamase specified by the resistance factor R-1818 in Escherichia coli K12 and other Gram-negative bacteria

1971 ◽  
Vol 123 (4) ◽  
pp. 501-505 ◽  
Author(s):  
J. W. Dale
Keyword(s):  
Escherichia Coli ◽  
Host Species ◽  
Host Bacterium ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
E Coli ◽  
R Factor ◽  
Relationship Of ◽  
The Relationship

1. The amino acid composition of the β-lactamase from E. coli (R-1818) was determined. 2. The R-1818 β-lactamase is inhibited by formaldehyde, hydroxylamine, sodium azide, iodoacetamide, iodine and sodium chloride. 3. The Km values for benzylpenicillin, ampicillin and oxacillin have been determined by using the R-factor enzyme from different host species. The same values were obtained, irrespective of the host bacterium. 4. The molecular weight of the enzyme was found to be 44600, and was the same for all host species. 5. The relationship of R-1818 and R-GN238 β-lactamases is discussed.

scholarly journals Purification and parcial characterization of a hemagglutinating factor (HAF): a possible adhesive factor of the diffuse adherent of Escherichia coli (DAEC)

1996 ◽  
Vol 38 (6) ◽  
pp. 401-406 ◽  
Author(s):  
Yano Tomomasa ◽  
Cleide Ferreira Catani ◽  
Michiko Arita ◽  
Takeshi Honda ◽  
Toshio Miwatani
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Hela Cells ◽  
Immunofluorescence Test ◽  
Native Form ◽  
Bacterial Surface ◽  
E Coli ◽  
Sds Page ◽  
Adhesive Factor

The mannose-resistant hemagglutinating factor (HAF) was extracted and purified from a diffuse adherent Escherichia coli (DAEC) strain belonging to the classic enteropathogenic E. coli (EPEC) serotype (0128). The molecular weight of HAF was estimated to be 18 KDa by SDS-PAGE and 66 KDa by Sephadex G100, suggesting that the native form of HAF consists of 3-4 monomeric HAF. Gold immunolabeling with specific HAF antiserum revealed that the HAF is not a rigid structure like fimbriae on the bacterial surface. The immunofluorescence test using purified HAF on HeLa cells, in addition to the fact that the HAF is distributed among serotypes of EPEC, suggests that HAF is a possible adhesive factor of DAEC strains

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