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Two DNA aptamers against avian influenza H9N2 virus prevent viral infection in cells.

Zhang Y, Yu Z, Jiang F, Fu P, Shen J, Wu W, Li J - PLoS ONE (2015)

Bottom Line: Both aptamers had whole-virus binding affinity.Also, an enzyme-linked aptamer assay (ELAA) confirmed binding affinity and specificity against other AIV subtypes.Our data provide a foundation for future development of innovative anti-influenza drugs.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Rapid Diagnostic Technology for Animal Disease, College of Veterinary Medicine, China Agricultural University, Beijing, P. R. China; Key Laboratory of Animal Epidemiology and Zoonosis, Ministry of Agriculture, College of Veterinary Medicine, China Agricultural University, Beijing, P. R. China.

ABSTRACT
New antiviral therapy for pandemic influenza mediated by the H9N2 avian influenza virus (AIV) is increasingly in demand not only for the poultry industry but also for public health. Aptamers are confirmed to be promising candidates for treatment and prevention of influenza viral infections. Thus, we studied two DNA aptamers, A9 and B4, selected by capillary electrophoresis-based systemic evolution of ligands by exponential enrichment (CE-SELEX) procedure using H9N2 AIV purified haemagglutinin (HA) as target. Both aptamers had whole-virus binding affinity. Also, an enzyme-linked aptamer assay (ELAA) confirmed binding affinity and specificity against other AIV subtypes. Finally, we studied aptamer-inhibitory effects on H9N2 AIV infection in Madin-Darby canine kidney (MDCK) cells and quantified viral load in supernatant and in cell with quantitative PCR (qPCR). Our data provide a foundation for future development of innovative anti-influenza drugs.

No MeSH data available.


Related in: MedlinePlus

Binding specificity of A9 and B4.(a) Specificity test in ELAA using HA proteins and whole viruses of various AIV subtypes. v, whole virus; p, purified HA protein; rp, recombinant HA protein. (b) Competitive ELAA using the corresponding unlabeled aptamer. Non, none of the unlabeled aptamer and biotin labeled aptamer was used.
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pone.0123060.g005: Binding specificity of A9 and B4.(a) Specificity test in ELAA using HA proteins and whole viruses of various AIV subtypes. v, whole virus; p, purified HA protein; rp, recombinant HA protein. (b) Competitive ELAA using the corresponding unlabeled aptamer. Non, none of the unlabeled aptamer and biotin labeled aptamer was used.

Mentions: HA proteins or whole viruses of various AIV subtypes were used in ELAA to confirm affinity specificity of A9 and B4. Data depicted in Fig 5A suggest that aptamers incubated with the HA or subtype H9 whole AIV had higher binding affinities than aptamers incubated with other subtypes. In addition, as measured by c-ELAA, when the concentration of the unlabeled aptamers increased to 200 nM, high competitive inhibition of A9 (76.3%) and B4 (66.7%) were observed. Thus it was suggested that both A9 and B4 could specifically bind to H9 AIV.


Two DNA aptamers against avian influenza H9N2 virus prevent viral infection in cells.

Zhang Y, Yu Z, Jiang F, Fu P, Shen J, Wu W, Li J - PLoS ONE (2015)

Binding specificity of A9 and B4.(a) Specificity test in ELAA using HA proteins and whole viruses of various AIV subtypes. v, whole virus; p, purified HA protein; rp, recombinant HA protein. (b) Competitive ELAA using the corresponding unlabeled aptamer. Non, none of the unlabeled aptamer and biotin labeled aptamer was used.
© Copyright Policy
Related In: Results  -  Collection

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Show All Figures
getmorefigures.php?uid=PMC4380446&req=5

pone.0123060.g005: Binding specificity of A9 and B4.(a) Specificity test in ELAA using HA proteins and whole viruses of various AIV subtypes. v, whole virus; p, purified HA protein; rp, recombinant HA protein. (b) Competitive ELAA using the corresponding unlabeled aptamer. Non, none of the unlabeled aptamer and biotin labeled aptamer was used.
Mentions: HA proteins or whole viruses of various AIV subtypes were used in ELAA to confirm affinity specificity of A9 and B4. Data depicted in Fig 5A suggest that aptamers incubated with the HA or subtype H9 whole AIV had higher binding affinities than aptamers incubated with other subtypes. In addition, as measured by c-ELAA, when the concentration of the unlabeled aptamers increased to 200 nM, high competitive inhibition of A9 (76.3%) and B4 (66.7%) were observed. Thus it was suggested that both A9 and B4 could specifically bind to H9 AIV.

Bottom Line: Both aptamers had whole-virus binding affinity.Also, an enzyme-linked aptamer assay (ELAA) confirmed binding affinity and specificity against other AIV subtypes.Our data provide a foundation for future development of innovative anti-influenza drugs.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Rapid Diagnostic Technology for Animal Disease, College of Veterinary Medicine, China Agricultural University, Beijing, P. R. China; Key Laboratory of Animal Epidemiology and Zoonosis, Ministry of Agriculture, College of Veterinary Medicine, China Agricultural University, Beijing, P. R. China.

ABSTRACT
New antiviral therapy for pandemic influenza mediated by the H9N2 avian influenza virus (AIV) is increasingly in demand not only for the poultry industry but also for public health. Aptamers are confirmed to be promising candidates for treatment and prevention of influenza viral infections. Thus, we studied two DNA aptamers, A9 and B4, selected by capillary electrophoresis-based systemic evolution of ligands by exponential enrichment (CE-SELEX) procedure using H9N2 AIV purified haemagglutinin (HA) as target. Both aptamers had whole-virus binding affinity. Also, an enzyme-linked aptamer assay (ELAA) confirmed binding affinity and specificity against other AIV subtypes. Finally, we studied aptamer-inhibitory effects on H9N2 AIV infection in Madin-Darby canine kidney (MDCK) cells and quantified viral load in supernatant and in cell with quantitative PCR (qPCR). Our data provide a foundation for future development of innovative anti-influenza drugs.

No MeSH data available.


Related in: MedlinePlus