ArticleJournal of virology2007
Fusion promotion by a paramyxovirus hemagglutinin-neuraminidase protein: pH modulation of receptor avidity of binding sites I and II.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 43 citations in OpenAlex.
- Human parainfluenza virus 3 fusion protein cleavage: a key determinant of infection and spread.Journal of virology · 2026Article
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- Epidemiological and molecular characteristics of human parainfluenza virus in southern China during 2016-2020.Virologica Sinica · 2025Article
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- Functional and structural basis of human parainfluenza virus type 3 neutralization with human monoclonal antibodies.Nature microbiology · 2024Article
- Unraveling dynamics of paramyxovirus-receptor interactions using nanoparticles displaying hemagglutinin-neuraminidase.PLoS pathogens · 2024Article
- Human parainfluenza virus evolution during lung infection of immunocompromised individuals promotes viral persistence.The Journal of clinical investigation · 2021Article
- Engineering Protease-Resistant Peptides to Inhibit Human Parainfluenza Viral Respiratory Infection.Journal of the American Chemical Society · 2021Article
- Parainfluenza virus entry at the onset of infection.Advances in virus research · 2021Article
- Human parainfluenza virus fusion complex glycoproteins imaged in action on authentic viral surfaces.PLoS pathogens · 2020Article
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- Inhibiting Human Parainfluenza Virus Infection by Preactivating the Cell Entry Mechanism.mBio · 2019Article
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- Circulating clinical strains of human parainfluenza virus reveal viral entry requirements for in vivo infection.Journal of virology · 2014Article
- Entry of Newcastle Disease Virus into the host cell: role of acidic pH and endocytosis.Biochimica et biophysica acta · 2014Article
- Measles virus fusion machinery activated by sialic acid binding globular domain.Journal of virology · 2013Article
- Identification of a region in the stalk domain of the nipah virus receptor binding protein that is critical for fusion activation.Journal of virology · 2013Article
- Regulation of paramyxovirus fusion activation: the hemagglutinin-neuraminidase protein stabilizes the fusion protein in a pretriggered state.Journal of virology · 2012Article
- The second receptor binding site of the globular head of the Newcastle disease virus hemagglutinin-neuraminidase activates the stalk of multiple paramyxovirus receptor binding proteins to trigger fusion.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Paramyxoviruses, including the childhood respiratory pathogen human parainfluenza virus type 3 (HPIV3), possess an envelope protein hemagglutinin-neuraminidase (HN) that has receptor-cleaving (neuraminidase), as well as receptor-binding, activity. HN is a type II transmembrane glycoprotein, present on the surface of the virus as a tetramer composed of two dimers. HN is also essential for activating the fusion protein (F) to mediate merger of the viral envelope with the host cell membrane. This initial step of viral entry occurs at the host cell surface at neutral pH. The HN molecule carries out these three different critical activities at specific points in the process of viral entry, and understanding the regulation of these activities is key for the design of strategies that block infection. One bifunctional site (site I) on the HN of HPIV3 possesses both receptor binding and neuraminidase activities, and we recently obtained experimental evidence for a second receptor binding site (site II) on HPIV3 HN. Mutation of HN at specific residues at this site, which is next to the HN dimer interface, confers enhanced fusion properties, without affecting neuraminidase activity or receptor binding at neutral pH. We now demonstrate that mutations at this site II, as well as at site I, confer pH dependence on HN's receptor avidity. These mutations permit pH to modulate the binding and fusion processes of the virus, potentially providing regulation at specific stages of the viral life cycle.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.