ArticleBioMed research international2013
Soluble form of canine transferrin receptor inhibits canine parvovirus infection in vitro and in vivo.
Article in BioMed research international, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Overview of Recent Advances in Canine Parvovirus Research: Current Status and Future Perspectives.Microorganisms · 2024Review
- Increased survival in puppies affected by Canine Parvovirus type II using an immunomodulator as a therapeutic aid.Scientific reports · 2021Article
- Crossing the Iron Gate: Why and How Transferrin Receptors Mediate Viral Entry.Annual review of nutrition · 2018Review
- Transcriptome profiling indicating canine parvovirus type 2a as a potential immune activator.Virus genes · 2016Article
- Molecular cloning of chicken IL-7 and characterization of its antiviral activity against IBDV in vivo.Poultry science · 2016Article
- Profiling of Host Cell Response to Successive Canine Parvovirus Infection Based on Kinetic Proteomic Change Identification.Scientific reports · 2016Article
- Nickel induces interleukin-1β secretion via the NLRP3-ASC-caspase-1 pathway.Inflammation · 2014Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Canine parvovirus (CPV) disease is an acute, highly infectious disease threatening the dog-raising industry. So far there are no effective therapeutic strategies to control this disease. Although the canine transferrin receptor (TfR) was identified as a receptor for CPV infection, whether extracellular domain of TfR (called soluble TfR (sTfR)) possesses anti-CPV activities remains elusive. Here, we used the recombinant sTfR prepared from HEK293T cells with codon-optimized gene structure to investigate its anti-CPV activity both in vitro and in vivo. Our results indicated that codon optimization could significantly improve sTfR expression in HEK293T cells. The prepared recombinant sTfR possessed a binding activity to both CPV and CPV VP2 capsid proteins and significantly inhibited CPV infection of cultured feline F81 cells and decreased the mortality of CPV-infected dogs, which indicates that the sTfR has the anti-CPV activity both in vitro and in vivo.
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Registered trials
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