In vivo andin vitro cloning and phenotype characterization of tellurite resistance determinant conferred by plasmid pTE53 of a clinical isolate ofEscherichia coli

1998 ◽  
Vol 43 (6) ◽  
pp. 589-599 ◽  
Author(s):  
J. Burian ◽  
Nguyen Tu ◽  
L'. Kl'učár ◽  
L. Guller ◽  
G. Lloyd-Jones ◽  
...  
2006 ◽  
Vol 51 (1) ◽  
pp. 359-360 ◽  
Author(s):  
Aki Okazaki ◽  
Matthew B. Avison

ABSTRACT We report the characterization of an intrinsic, chromosomally carried aph(3′)-IIc gene from Stenotrophomonas maltophilia clinical isolate K279a, encoding an aminoglycoside phosphotransferase enzyme that significantly increases MICs of kanamycin, neomycin, butirosin, and paromomycin when expressed in Escherichia coli. Disruption of aph(3′)-IIc in K279a results in decreased MICs of these drugs.


2002 ◽  
Vol 8 (4) ◽  
pp. 267-272 ◽  
Author(s):  
Amel Bellaaj ◽  
Claude Bollet ◽  
Nejib Alfeddy ◽  
Ferid Limam ◽  
Cherifa Belhadj ◽  
...  

2006 ◽  
Vol 87 (6) ◽  
pp. 1643-1648 ◽  
Author(s):  
Fumio Seki ◽  
Makoto Takeda ◽  
Hiroko Minagawa ◽  
Yusuke Yanagi

Signalling lymphocyte activation molecule (SLAM) acts as a cellular receptor for Measles virus (MV). The recombinant MV, based on a SLAM-using clinical isolate in which asparagine at position 481 of the haemagglutinin was replaced with tyrosine, was generated. Characterization of this recombinant virus revealed that the N481Y substitution in the haemagglutinin allowed it to utilize CD46 as an alternative receptor, but that its ability to use CD46 was rather low in CD46+ SLAM− cell lines compared with that of the recombinant virus possessing the haemagglutinin of the Edmonston laboratory strain. Thus, an N481Y substitution alone may not be sufficient to make SLAM-using MVs use CD46 efficiently, suggesting that further substitutions in the haemagglutinin are required for them to grow efficiently in CD46+ cells like the Edmonston strain. This may be a reason why few CD46-using MVs are detected in vivo.


2020 ◽  
Vol 477 (7) ◽  
pp. 1261-1286 ◽  
Author(s):  
Marie Anne Richard ◽  
Hannah Pallubinsky ◽  
Denis P. Blondin

Brown adipose tissue (BAT) has long been described according to its histological features as a multilocular, lipid-containing tissue, light brown in color, that is also responsive to the cold and found especially in hibernating mammals and human infants. Its presence in both hibernators and human infants, combined with its function as a heat-generating organ, raised many questions about its role in humans. Early characterizations of the tissue in humans focused on its progressive atrophy with age and its apparent importance for cold-exposed workers. However, the use of positron emission tomography (PET) with the glucose tracer [18F]fluorodeoxyglucose ([18F]FDG) made it possible to begin characterizing the possible function of BAT in adult humans, and whether it could play a role in the prevention or treatment of obesity and type 2 diabetes (T2D). This review focuses on the in vivo functional characterization of human BAT, the methodological approaches applied to examine these features and addresses critical gaps that remain in moving the field forward. Specifically, we describe the anatomical and biomolecular features of human BAT, the modalities and applications of non-invasive tools such as PET and magnetic resonance imaging coupled with spectroscopy (MRI/MRS) to study BAT morphology and function in vivo, and finally describe the functional characteristics of human BAT that have only been possible through the development and application of such tools.


1995 ◽  
Vol 74 (02) ◽  
pp. 673-679 ◽  
Author(s):  
C E Dempfle ◽  
S A Pfitzner ◽  
M Dollman ◽  
K Huck ◽  
G Stehle ◽  
...  

SummaryVarious assays have been developed for quantitation of soluble fibrin or fibrin monomer in clinical plasma samples, since this parameter directly reflects in vivo thrombin action on fibrinogen. Using plasma samples from healthy blood donors, patients with cerebral ischemic insult, patients with septicemia, and patients with venous thrombosis, we compared two immunologic tests using monoclonal antibodies against fibrin-specific neo-epitopes, and two functional tests based on the cofactor activity of soluble fibrin complexes in tPA-induced plasminogen activation. Test A (Enzymun®-Test FM) showed the best discriminating power among normal range and pathological samples. Test B (Fibrinostika® soluble fibrin) clearly separated normal range from pathological samples, but failed to discriminate among samples from patients with low grade coagulation activation in septicemia, and massive activation in venous thrombosis. Functional test C (Fibrin monomer test Behring) displayed good discriminating power between normal and pathological range samples, and correlated with test A (r = 0.61), whereas assay D (Coa-Set® Fibrin monomer) showed little discriminating power at values below 10 μg/ml and little correlation with other assays. Standardization of assays will require further characterization of analytes detected.


Diabetes ◽  
1990 ◽  
Vol 39 (10) ◽  
pp. 1243-1250 ◽  
Author(s):  
L. Rossetti ◽  
A. Giaccari ◽  
E. Klein-Robbenhaar ◽  
L. R. Vogel

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