scholarly journals Single-point mutation detection in RNA extracts using gold nanoparticles modified with hydrophobic molecular beacon-like structures

2014 ◽  
Vol 50 (23) ◽  
pp. 3018-3020 ◽  
Author(s):  
Alfonso Latorre ◽  
Christian Posch ◽  
Yolanda Garcimartín ◽  
Susana Ortiz-Urda ◽  
Álvaro Somoza
Keyword(s):  
Gold Nanoparticles ◽  
Point Mutation ◽  
Mutation Detection ◽  
Molecular Beacon ◽  
Single Point ◽  
Point Mutations ◽  
Single Point Mutation ◽  
Target Sequence ◽  
Cholesterol Derivative ◽  
Single Point Mutations

The functionalization of gold nanoparticles with a cholesterol derivative affords a sensor that is able to detect single-point mutations. The solubility of the nanoparticles is modulated by the presence of the target sequence inducing its aggregation.

Few molecule SERS detection using nanolens based plasmonic nanostructure: application to point mutation detection

RSC Advances ◽  
2016 ◽  
Vol 6 (109) ◽  
pp. 107916-107923 ◽  
Author(s):  
Gobind Das ◽  
Salma Alrasheed ◽  
Maria Laura Coluccio ◽  
Francesco Gentile ◽  
Annalisa Nicastri ◽  
...  
Keyword(s):  
Point Mutation ◽  
Mutation Detection ◽  
Single Point ◽  
Point Mutations ◽  
Plasmonic Nanostructure ◽  
Sers Detection ◽  
Self Similar ◽  
Single Point Mutations

Self-similar chain based nanolens plasmonic devices were fabricated for detecting single point mutations.

Protein Adsorption and Reorganization on Nanoparticles Probed by the Coffee-Ring Effect: Application to Single Point Mutation Detection

2016 ◽  
Vol 138 (36) ◽  
pp. 11623-11632 ◽  
Author(s):  
Stéphanie Devineau ◽  
Manos Anyfantakis ◽  
Laurent Marichal ◽  
Laurent Kiger ◽  
Mathieu Morel ◽  
...  
Keyword(s):  
Protein Adsorption ◽  
Point Mutation ◽  
Mutation Detection ◽  
Single Point ◽  
Single Point Mutation ◽  
Coffee Ring ◽  
Coffee Ring Effect ◽  
Ring Effect

Single point mutation detection in living cancer cells by far-red emitting PNA–FIT probes

2016 ◽  
Vol 52 (11) ◽  
pp. 2405-2407 ◽  
Author(s):  
N. Kolevzon ◽  
D. Hashoul ◽  
S. Naik ◽  
A. Rubinstein ◽  
E. Yavin
Keyword(s):  
Cancer Cells ◽  
Point Mutation ◽  
Mutation Detection ◽  
Single Point ◽  
Living Cells ◽  
Single Point Mutation ◽  
Snp Detection ◽  
First Time

SNP detection of the mutated kRAS oncogene in living cells is shown to be achieved for the first time by cell-permeable and far-red emitting PNA–FIT probes.

Glanzmann Mutations : New Allelic Variants and Role of the β3 Lys253 in the αIIb/β3 Interaction Highlighted by the Lys253Met Substitution.

Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 1312-1312
Author(s):  
Vincent Jallu ◽  
Alexandre De Brevern ◽  
Simon Panzer ◽  
Marie-Francoise Torchet ◽  
Cecile Kaplan-Gouet
Keyword(s):  
Rna Processing ◽  
Conflicts Of Interest ◽  
Single Point ◽  
Point Mutations ◽  
Single Point Mutation ◽  
Platelet Surface ◽  
Cos Cells ◽  
Single Point Mutations ◽  
Complex Expression

Abstract Abstract 1312 Poster Board I-336 Introduction Glanzmann thrombasthenia (GT) is an autosomal recessive inherited bleeding disorder characterized by an impaired platelet aggregation. GT results from defects of the platelet fibrinogen receptor αIIbβ3. GT mutations provide useful tools for structure-function relationship studies of αIIbβ3. Patient and methods Genomic DNA from 6 patients has been amplified for αIIb and β3 promoters and exons sequences. PCR products were directly sequenced. Potential RNA processing alterations have been studied in silico by using Genscan, NNSPLICE and ESEFinder online tools. When no RNA splicing anomaly was predicted, the effect of single point mutation on αIIbβ3 expression has been studied by using transiently transfected Cos cells. Finally, structural consequences of amino acid substitutions has been studied using the published model of αIIbβ3 (code PDB 2VDL) and structural modelling. Results 7 new mutations have been characterized. 1 deletion / insertion, 2 single point mutations inducing stop codon and 1 resulting in splicing site disruption were identified. The 3 last identified single point mutations were not predicted to affect normal RNA processing but has been shown to prevent normal expression of mutant αIIbβ3 at the surface of Cos cells. The p.Meth118Arg and p.Gly221Asp substitutions that induce both important steric hindrance and charge modifications, are located inside the β-I domain of β3. So they should deeply alter the proper folding of the β-I domain, preventing the complex expression at the platelet surface. On the other hand, the p.Lys253Met protrudes from the β-I domain toward the αIIb β-propeller. A structural model of the Met253 β-I mutant has been done. An estimation of the direct electrostatic and desolvation free energies of interaction between the β-I domain surface and the αIIb β-propeller indicated that rather than the presence of a methionine, it is the lost of the Lys253 which is responsible for the complex expression defect. Conclusion Seven new GT mutations have been identified and the p.Lys253Met substitution helped to define a key role of the Lys253 in the αIIb β-propeller / β3 β-I domains interaction. Disclosures No relevant conflicts of interest to declare.

scholarly journals An integrated multi-molecular sensor for simultaneous BRAFV600E protein and DNA single point mutation detection in circulating tumour cells

Lab on a Chip ◽  
2019 ◽  
Vol 19 (5) ◽  
pp. 738-748 ◽  
Author(s):  
Shuvashis Dey ◽  
Kevin M. Koo ◽  
Zhaoran Wang ◽  
Abu A. I. Sina ◽  
Alain Wuethrich ◽  
...  
Keyword(s):  
Point Mutation ◽  
Mutation Detection ◽  
Biological Fluids ◽  
Single Point ◽  
Single Point Mutation ◽  
Circulating Tumour Cells ◽  
Cell Capture ◽  
Entire Sample ◽  
Molecular Sensor ◽  
On Chip

We report an integrated multi-molecular sensor (IMMS) platform for an entire sample-to-answer protocol encompassing melanoma cell capture in biological fluids, on-chip cell lysis, and combined quantification of intracellular BRAFV600E DNA and protein amounts.

scholarly journals Specific point mutations in Lactobacillus casei ATCC 27139 cause a phenotype switch from Lac− to Lac+

Microbiology ◽  
2009 ◽  
Vol 155 (3) ◽  
pp. 751-760 ◽  
Author(s):  
Yu-Kuo Tsai ◽  
Hung-Wen Chen ◽  
Ta-Chun Lo ◽  
Thy-Hou Lin
Keyword(s):  
Gene Cluster ◽  
Point Mutation ◽  
Lactobacillus Casei ◽  
Stop Codon ◽  
Single Point ◽  
Point Mutations ◽  
Premature Stop Codon ◽  
Gene Clusters ◽  
Single Point Mutation ◽  
Phenotype Switch

Lactose metabolism is a changeable phenotype in strains of Lactobacillus casei. In this study, we found that L. casei ATCC 27139 was unable to utilize lactose. However, when exposed to lactose as the sole carbon source, spontaneous Lac+ clones could be obtained. A gene cluster (lacTEGF–galKETRM) involved in the metabolism of lactose and galactose in L. casei ATCC 27139 (Lac−) and its Lac+ revertant (designated strain R1) was sequenced and characterized. We found that only one nucleotide, located in the lacTEGF promoter (lacTp), of the two lac–gal gene clusters was different. The protein sequence identity between the lac–gal gene cluster and those reported previously for some L. casei (Lac+) strains was high; namely, 96–100 % identity was found and no premature stop codon was identified. A single point mutation located within the lacTp promoter region was also detected for each of the 41 other independently isolated Lac+ revertants of L. casei ATCC 27139. The revertants could be divided into six classes based on the positions of the point mutations detected. Primer extension experiments conducted on transcription from lacTp revealed that the lacTp promoter of these six classes of Lac+ revertants was functional, while that of L. casei ATCC 27139 was not. Northern blotting experiments further confirmed that the lacTEGF operon of strain R1 was induced by lactose but suppressed by glucose, whereas no blotting signal was ever detected for L. casei ATCC 27139. These results suggest that a single point mutation in the lacTp promoter was able to restore the transcription of a fully functional lacTEGF operon and cause a phenotype switch from Lac− to Lac+ for L. casei ATCC 27139.

Competitive assay to improve the specificity of detection of single-point mutations in alpha 1-antitrypsin deficiency

1993 ◽  
Vol 39 (10) ◽  
pp. 2157-2162 ◽  
Author(s):  
A Gunneberg ◽  
G Scobie ◽  
K Hayes ◽  
N Kalsheker
Keyword(s):  
Signal To Noise Ratio ◽  
Single Point ◽  
Point Mutations ◽  
Base Substitution ◽  
Single Point Mutation ◽  
Antitrypsin Deficiency ◽  
Alpha 1 Antitrypsin Deficiency ◽  
Single Point Mutations ◽  
Alpha 1 Antitrypsin ◽  
Lower Temperature

Abstract Allele-specific oligonucleotides are used widely for the detection of single point mutations in genes. A modification of this assay based on competition has been developed for detection of the Z mutation of alpha 1-antitrypsin (alpha 1-AT). The normal alpha 1-AT allele is referred to as M, and the Z mutation arises from a single base substitution. Amplified DNA products corresponding to homozygous M, heterozygous MZ, and homozygous Z obtained by the polymerase chain reaction were incubated with a twofold molar excess of unlabeled oligonucleotide prior to hybridization with a radiolabeled oligonucleotide. Thus, initial incubation with unlabeled M-specific oligonucleotide was followed by hybridization with radiolabeled Z-specific oligonucleotide, and vice versa. This assay increased the specificity of single-point mutation detection three- to four-fold. Furthermore, specific hybridization was obtained at a lower temperature as a consequence of improving the signal-to-noise ratio.

scholarly journals A Mathematical Graph-Theoretic Model of Single Point Mutations Associated with Sickle Cell Anemia Disease

2021 ◽  
Vol 9 ◽  
pp. 1-14
Author(s):  
Edem K. Netsey ◽  
Dr. samuel Kakraba ◽  
Samuel M. Naandam ◽  
Aayire C. Yadem
Keyword(s):  
Sickle Cell ◽  
Sickle Cell Anemia ◽  
Single Point ◽  
Point Mutations ◽  
Sub Saharan Africa ◽  
Single Point Mutation ◽  
Theoretic Model ◽  
Related Disorder ◽  
Graph Theoretic ◽  
Single Point Mutations

Many diseases like cystic fibrosis and sickle cell anemia disease (SCD), among others, arise from single point mutations in the respective proteins. How a single point mutation might lead to a global devastating consequence on a protein remains an intellectual mystery. SCD is a genetic blood-related disorder resulting from mutations in the beta chain of the human hemoglobin protein (simply, β-globin), subsequently affecting the entire human body. Higher mortality and morbidity rates have been reported for patients with SCD, especially in sub-Saharan Africa. Clinical management of SCD often requires specialized interdisciplinary clinicians. SCD presents a major global burden, hence an improved understanding of how single point mutations in β-globin results in different phenotypes of SCD might offer insight into protein engineering, with potential therapeutic intervention in view. By use of mathematical modeling, we built a hierarchical (nested) graph-theoretic model for the β-globin. Subsequently, we quantified the network of interacting amino acid residues, representing them as molecular system of three distinct stages (levels) of interactions. Using our nested graph model, we studied the effect of virtual single point mutations in β-globin that results in varying phenotypes of SCD, visualized by unsupervised machine learning algorithm, the dendrogram.

scholarly journals Increasing Prevalence of Quinolone Resistance in Human Nontyphoid Salmonella enterica Isolates Obtained in Spain from 1981 to 2003

2004 ◽  
Vol 48 (10) ◽  
pp. 3789-3793 ◽  
Author(s):  
José M. Marimón ◽  
María Gomáriz ◽  
Carmen Zigorraga ◽  
Gustavo Cilla ◽  
Emilio Pérez-Trallero
Keyword(s):  
Nalidixic Acid ◽  
Point Mutation ◽  
Salmonella Enterica ◽  
Single Point ◽  
Point Mutations ◽  
Fluoroquinolone Resistance ◽  
Human Consumption ◽  
Single Point Mutation ◽  
Gene Coding ◽  
Serovar Typhimurium

ABSTRACT From January 1981 to December 2003, susceptibility to nalidixic acid was tested in 10,504 nontyphoid Salmonella enterica isolates from patients with acute enteric disease in Gipuzkoa, Spain. The prevalence of nalidixic acid resistance steadily increased from less than 0.5% before 1991 to 38.5% in 2003, mainly due to the increase in resistance among isolates of the most prevalent serovar, S. enterica serovar Enteritidis. For nalidixic acid-resistant isolates, the ciprofloxacin MIC was eightfold higher than that for susceptible isolates, and the nalidixic acid-resistant isolates contained a single point mutation in the gyrA gene (at codons for Ser83 or Asp87). The same mutations were found in a sample of nalidixic acid-resistant nontyphoid Salmonella strains isolated between 1999 and 2003 from retail food for human consumption. In 2003, we identified five S. enterica serovar Typhimurium clinical isolates with high-level fluoroquinolone resistance (ciprofloxacin MIC, 16 μg/ml) with two point mutations in the gyrA gene (coding for Ser83→Phe and Asp87→Asn) and one point mutation in the parC gene (coding for Ser80→Arg). Strict sanitary controls are needed to avoid the spread of ciprofloxacin-resistant serovar Typhimurium isolates, and a more efficient veterinary policy must be adopted to decrease the large burden of Salmonella serovar Enteritidis infections in humans in our region.

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