ArticleScientific reports2017
The impact of the butterfly effect on human parainfluenza virus haemagglutinin-neuraminidase inhibitor design.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Leveraging human precision cut lung slices for the study of human parainfluenza virus 3 infection.Respiratory research · 2025Article
- Genetic characteristics of human parainfluenza viruses 1-4 associated with acute lower respiratory tract infection in Chinese children, during 2015-2021.Microbiology spectrum · 2024Article
- Functional and structural basis of human parainfluenza virus type 3 neutralization with human monoclonal antibodies.Nature microbiology · 2024Article
- Interplay of Modified Sialic Acid Inhibitors and the Human Parainfluenza Virus 1 Hemagglutinin-Neuraminidase Active Site.ACS medicinal chemistry letters · 2023Article
- Design, Synthesis, and Antiviral Evaluation of Sialic Acid Derivatives as Inhibitors of Newcastle Disease Virus Hemagglutinin-Neuraminidase: A Translational Study on Human Parainfluenza Viruses.ACS infectious diseases · 2023Article
- Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms.Science advances · 2023Article
- Targeting Human Parainfluenza Virus Type-1 Haemagglutinin-Neuraminidase with Mechanism-Based Inhibitors.Viruses · 2019Article
- Inhibition of sialidase activity as a therapeutic approach.Drug design, development and therapy · 2018Review
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5 authors.
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Abstract
Human parainfluenza viruses represent a leading cause of lower respiratory tract disease in children, with currently no available approved drug or vaccine. The viral surface glycoprotein haemagglutinin-neuraminidase (HN) represents an ideal antiviral target. Herein, we describe the first structure-based study on the rearrangement of key active site amino acid residues by an induced opening of the 216-loop, through the accommodation of appropriately functionalised neuraminic acid-based inhibitors. We discovered that the rearrangement is influenced by the degree of loop opening and is controlled by the neuraminic acid's C-4 substituent's size (large or small). In this study, we found that these rearrangements induce a butterfly effect of paramount importance in HN inhibitor design and define criteria for the ideal substituent size in two different categories of HN inhibitors and provide novel structural insight into the druggable viral HN protein.
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