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1.
Balkan J Med Genet ; 20(1): 91-94, 2017 Jun 30.
Article in English | MEDLINE | ID: mdl-28924546

ABSTRACT

Sirenomelia, also known as "mermaid malformation/syndrome," is a rare, serious congenital anomaly characterized by variable degrees of fusion of the lower limbs and associated with severe malformations of vertebral, genitourinary, cardiovascular system and single umbilical artery. The first pregnancy of a 25-year-old woman resulted in one twin born by Cesarian section at 32 weeks' gestation, who was referred to our hospital with cyanosis, a congenital anomaly and respiratory distress. On physical examination, there was no urogenital region and anal fissure and gender was indeterminate. The arms were in adduction and wrist in flexion position with four fingers on the right hand and two fingers on the left hand. There was a single lower extremity with a webbed single foot and two toes consistent with sirenomelia type IV radiologically. Abdominal ultrasonography showed urogenital system agenesis and echocardiography detected hypoplastic left heart. However, the patient died 4 hours after birth. The other twin was followed for 1 week for nutrition and respiratory support and was then discharged without any problems.

4.
Lett Appl Microbiol ; 57(4): 362-7, 2013 Oct.
Article in English | MEDLINE | ID: mdl-23789811

ABSTRACT

UNLABELLED: In this study, a total of 180 vegetable samples collected from several district bazaars of Istanbul were investigated for the occurrence of Escherichia coli using a culture-based method. The isolates were subjected to real-time PCR detection of Shiga-toxin-producing E. coli (STEC) using primers specific for the Shiga toxin (stx1 and stx2) and intimin (eae) virulence genes. The prevalences of E. coli in the samples were 93·3% in spinach, 93·3% in lettuce, 86·6% in parsley, 43·3% in carrot, 33·3% in cucumber and 13·3% in tomato. Of 180 samples, 13 contained STEC (six parsley, three carrots, three lettuces and one cucumber of 30 samples of each). Among 13 STEC-positive isolates, presence of stx1, stx2 and eae was detected in only one sample, stx2 and eae in two samples, and stx2 in ten samples. Serotype O157 was found in parsley, lettuce and carrot; O26 in lettuce, parsley, cucumber and carrot; and O111 and O113 in parsley only. In conclusion, STEC was present in vegetable samples marketed in several district bazaars in Istanbul; this might represent a route of transmission of pathogenic STEC to humans and be harmful to public health. SIGNIFICANCE AND IMPACT OF THE STUDY: We assessed the occurrence of virulent Escherichia (E.) coli and Shiga-toxin-producing E. coli (STEC) virulent populations in the vegetable samples collected from several district bazaars in Istanbul, Turkey. The results indicated that the vegetables from the bazaars had poor microbial quality and represented a potential health risk to customers.


Subject(s)
Food Microbiology , Real-Time Polymerase Chain Reaction/methods , Shiga-Toxigenic Escherichia coli/isolation & purification , Vegetables/microbiology , DNA Primers/genetics , Escherichia coli O157/classification , Escherichia coli O157/genetics , Escherichia coli O157/isolation & purification , Escherichia coli Proteins/genetics , Shiga Toxin/genetics , Shiga-Toxigenic Escherichia coli/classification , Shiga-Toxigenic Escherichia coli/genetics , Turkey , Virulence Factors/genetics
5.
J Mol Biol ; 304(4): 621-32, 2000 Dec 08.
Article in English | MEDLINE | ID: mdl-11099384

ABSTRACT

Colicins translocate across the Escherichia coli outer membrane and periplasm by interacting with several receptors. After first binding to the outer membrane surface receptors via their central region, they interact with TolA or TonB proteins via their N-terminal region. Colicin N residues critical to TolA binding have been discovered, but the full extent of any colicin TolA site is unknown. We present, for the first time, a fully mapped TolA binding site for a colicin. It was determined through the use of alanine-scanning mutants, glutathione S-transferase fusion peptides and Biacore/fluorescence binding studies. The minimal TolA binding region is 27 residues and of similar size to the TolA binding region of bacteriophage g3p-D1 protein. Stopped-flow kinetic studies show that the binding to TolA follows slow association kinetics. The role of other E. coli Tol proteins in colicin translocation was also investigated. Isothermal titration microcalorimetry (ITC) and in vivo studies conclusively show that colicin N translocation does not require the presence of TolB. ITC also demonstrated colicin A interaction with TolB, and that colicin A in its native state does not interact with TolAII-III. Colicin N does not bind TolR-II. The TolA protein is shown to be unsuitable for direct immobilisation in Biacore analysis.


Subject(s)
Bacterial Proteins/metabolism , Colicins/chemistry , Colicins/metabolism , Escherichia coli Proteins , Escherichia coli/chemistry , Periplasmic Proteins , Surface Plasmon Resonance , Amino Acid Sequence , Amino Acid Substitution/genetics , Binding Sites , Calorimetry , Circular Dichroism , Colicins/genetics , Fluorescence , Kinetics , Molecular Sequence Data , Mutation/genetics , Protein Binding , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/metabolism , Sequence Alignment , Titrimetry , Tryptophan/genetics , Tryptophan/metabolism
6.
FEBS Lett ; 431(3): 305-8, 1998 Jul 24.
Article in English | MEDLINE | ID: mdl-9714531

ABSTRACT

Beta-barrel pores are found in outer membrane porins of gram-negative bacteria, bacterial toxins and mitochondrial channels. Apart from the beta-barrel the three groups show no close sequence or structural homology but these pores exhibit symmetrical voltage gating when reconstituted into planar lipid bilayers. The structures of several of these are known and many site-directed mutants have been examined. As a result it seems evident that the gating is a common characteristic of these unrelated large pores and is not generated by specialised structures in the pore lumen.


Subject(s)
Bacterial Toxins/metabolism , Ion Channel Gating , Porins/metabolism , Bacterial Toxins/chemistry , Porins/chemistry , Protein Conformation
7.
FEBS Lett ; 411(2-3): 201-5, 1997 Jul 14.
Article in English | MEDLINE | ID: mdl-9271205

ABSTRACT

Three sulfhydryl labels were used to modify two mutated sites, R37C and R74C in the eyelet of the outer membrane porin OmpC. Modification of R37C with the neutral groups Aldrithiol and bimane increases thermal stability but the negatively charged iodoacetate causes a decrease in thermal stability. The effects of substitution at R74C were less significant. Bimane labelling increases the voltage sensitivity and decreases the single channel conductance at R37C asymmetrically with smaller channels being recorded at cis negative voltages. Negatively charged acetate does not affect the voltage gating.


Subject(s)
Bacterial Outer Membrane Proteins/chemistry , Cysteine/chemistry , Escherichia coli/chemistry , Porins/chemistry , Bacterial Outer Membrane Proteins/genetics , Bacterial Outer Membrane Proteins/metabolism , Bridged Bicyclo Compounds/metabolism , Circular Dichroism , Cysteine/metabolism , Electrophoresis, Polyacrylamide Gel , Electrophysiology , Ion Channel Gating , Models, Molecular , Mutation , Porins/genetics , Porins/metabolism , Protein Conformation , Protein Denaturation , Spectrometry, Fluorescence , Sulfhydryl Reagents/pharmacology , Temperature
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