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Indolopyridones inhibit human immunodeficiency virus reverse transcriptase with a novel mechanism of action
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Jochmans D Deval J Kesteleyn B Van Marck H Bettens E De Baere I Dehertogh P Ivens T Van Ginderen M Van Schoubroeck B Ehteshami M Wigerinck P Götte M Hertogs K 《Journal of virology》2006,80(24):12283-12292
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Interaction of C5 protein with RNA aptamers selected by SELEX 总被引:1,自引:0,他引:1
RNA aptamers binding to C5 protein, the protein component of Escherichia coli RNase P, were selected and characterized as an initial step in elucidating the mechanism of action of C5 protein as an RNA-binding protein. Sequence analyses of the RNA aptamers suggest that C5 protein binds various RNA molecules with dissociation constants comparable to that of M1 RNA, the RNA component of RNase P. The dominant sequence, W2, was chosen for further study. Interactions between W2 and C5 protein were independent of Mg2+, in contrast to the Mg2+ dependency of M1 RNA–C5 protein interactions. The affinity of W2 for C5 protein increased with increasing concentration of monovalent NH4+, suggesting interactions via hydrophobic attraction. W2 forms a fairly stable complex with C5 protein, although the stability of this complex is lower than that of the complex of M1 RNA with C5 protein. The core RNA motif essential for interaction with C5 protein was identified as a stem–loop structure, comprising a 5 bp stem and a 20 nt loop. Our results strongly imply that C5 protein is an interacting partner protein of some cellular RNA species apart from M1 RNA. 相似文献
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Hari P. Dwivedi R. Derike Smiley Lee-Ann Jaykus 《Applied microbiology and biotechnology》2010,87(6):2323-2334
The need for pre-analytical sample processing prior to the application of rapid molecular-based detection of pathogens in
food and environmental samples is well established. Although immunocapture has been applied in this regard, alternative ligands
such as nucleic acid aptamers have advantages over antibodies such as low cost, ease of production and modification, and comparable
stability. To identify DNA aptamers demonstrating binding specificity to Campylobacter jejuni cells, a whole-cell Systemic Evolution of Ligands by EXponential enrichment (SELEX) method was applied to a combinatorial
library of FAM-labeled single-stranded DNA molecules. FAM-labeled aptamer sequences with high binding affinity to C. jejuni A9a as determined by flow cytometric analysis were identified. Aptamer ONS-23, which showed particularly high binding affinity
in preliminary studies, was chosen for further characterization. This aptamer displayed a dissociation constant (K
d
value) of 292.8 ± 53.1 nM with 47.27 ± 5.58% cells fluorescent (bound) in a 1.48-μM aptamer solution. Binding assays to assess
the specificity of aptamer ONS-23 showed high binding affinity (25–36%) for all other C. jejuni strains screened (inclusivity) and low apparent binding affinity (1–5%) with non-C. jejuni strains (exclusivity). Whole-cell SELEX is a promising technique to design aptamer-based molecular probes for microbial pathogens
without tedious isolation and purification of complex markers or targets. 相似文献
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