ArticleMikrochimica acta2026
Fluorescent aptasensor targeting the fibrinogen-binding domain of clumping factor A for rapid detection of Staphylococcus aureus.
Article in Mikrochimica acta, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Staphylococcus aureus (S. aureus) is a versatile pathogen responsible for a wide range of illnesses from minor skin infections to critical conditions like pneumonia, sepsis, and toxic shock syndrome in humans. Clumping factor A (ClfA), a surface protein of S. aureus, plays a crucial role in bloodstream infections by attaching to fibrinogen, facilitating bacterial adherence and clumping. This study describes the selection of DNA aptamers, specific to ClfA using the technique of Ni-NTA affinity systematic evolution of ligands by exponential enrichment (SELEX). A DNA library of 76-mer single-stranded oligodeoxynucleotides with a 40-mer random region was utilized. The SELEX process involved thermal equilibration, incubation with ClfA immobilized on Ni-NTA beads, and multiple washing and elution steps. Oligonucleotide pool obtained from the final round was cloned and sequenced. Selected aptamers were validated using microtiter plate-based aptamer binding assay, molecular docking, electrophoretic mobility shift assay (EMSA), and bead-based binding assay. The aptamer (CA 11.1) binding affinity was determined by nonlinear regression analysis, yielding an apparent dissociation constant (K
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