ArticleVirology journal2018
Quantitative investigation of the direct interaction between Hemagglutinin and fusion proteins of Peste des petits ruminant virus using surface Plasmon resonance.
Article in Virology journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Development of a Colloidal Gold Immunochromatographic Test Strip for PPRV Antibody Detection Based on Antigenic Epitope-Derived Recombinant Protein.Animals : an open access journal from MDPI · 2026Article
- Synonymous codon usage influences the transmission of peste des petits ruminants (PPR) virus in camels.Veterinary research communications · 2024Article
- Identification of amino acid residues involved in the interaction betweenThe Journal of general virology · 2020Article
- Paradigm shift in the diagnosis of peste des petits ruminants: scoping review.Acta veterinaria Scandinavica · 2020Article
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Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe specific and dynamic interaction between the hemagglutinin (H) and fusion (F) proteins of morbilliviruses is a prerequisite for the conformational rearrangements and membrane fusion during infection process. The two heptad repeat regions (HRA and HRB) of F protein are both important for the triggering of F protein.
methodsIn this study, the direct interactions of Peste des petits ruminants virus (PPRV) H with F, HRA and HRB were quantitatively evaluated using biosensor surface plasmon resonance (SPR).
resultsThe binding affinities of immobilized pCMV-HA-H (HA-H) interacted with proteins pCMV-HA-F (HA-F) and pCMV-HA-HRB (HA-HRB) (K
conclusionsThe differences of the binding affinities suggested that HRB is involved in functionally important intermolecular interaction in the fusion process.
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Registered trials
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