ArticleApplied microbiology and biotechnology2021
Identification and characterization of DNA aptamers specific to VP2 protein of canine parvovirus.
Article in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Decoding sequence recognition code of nucleic acid-binding proteins of human-infecting DNA viruses.iMeta · 2026Article
- Exploring an Aptamer-Based Approach to Assess Canine Parvovirus Integrity After Disinfection Treatment.Viruses · 2025Article
- Aptamer and DNAzyme Based Colorimetric Biosensors for Pathogen Detection.Angewandte Chemie (International ed. in English) · 2025Review
- Whole-genome sequence analysis of canine parvovirus reveals replacement with a novel CPV-2c strain throughout India.Archives of virology · 2024Article
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Authors and funding
11 authors.
Funding
Abstract
Canine parvovirus-2 (CPV-2) is ubiquitously distributed in dog population worldwide causing a severe and often fatal gastroenteritis. Owing to its highly contagious nature, rapid detection of CPV is crucial in effective control of the disease. Aptamers have emerged as potential alternative to antibodies as affinity reagents in diagnostic field. Present study was aimed to select and validate ssDNA aptamers specific to CPV. Systematic evolution of ligands through exponential enrichment (SELEX) method was employed for selection of CPV structural protein (VP2) specific DNA aptamers. SELEX was performed using a pool of ssDNA library comprising 30 random nucleotide region. A total of seven rounds of SELEX were performed using VP2 protein as target antigen which yielded ten aptamers (1A-10A) with distinct sequences. Target binding of all ten aptamers was assessed by dot blot and enzyme-linked oligonucleotide assay (ELONA) which revealed that 5A, 6A, 9A, and 10A were superior binders. In silico analysis of the aptamers revealed the existence of binding site on VP2 protein, and binding pattern was similar to in vitro findings. The affinity (K
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