ArticleJournal of virology2005
Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion protein.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 69 citations in OpenAlex.
- Relevance of potential endocytosis motifs in Cedar virus glycoprotein G for its biological activity.Journal of virology · 2026Article
- Trafficking and Activation ofViruses · 2025Review
- Pseudotyped Virus for Henipavirus.Advances in experimental medicine and biology · 2023Review
- Adaptor complex-mediated trafficking of Newcastle disease virus fusion protein is regulated by the YLMY motif of its cytoplasmic tail.Virulence · 2022Article
- The role of N-linked glycosylation in proteolytic processing and cell surface transport of the Cedar virus fusion protein.Virology journal · 2022Article
- Article
- Third Helical Domain of the Nipah Virus Fusion Glycoprotein Modulates both Early and Late Steps in the Membrane Fusion Cascade.Journal of virology · 2020Article
- Article
- Disentangling Biomolecular Corona Interactions With Cell Receptors and Implications for Targeting of Nanomedicines.Frontiers in bioengineering and biotechnology · 2020Review
- Transmembrane Domain Dissociation Is Required for Hendra Virus F Protein Fusogenic Activity.Journal of virology · 2019Article
- Fusogenicity of the Ghana Virus (Viruses · 2019Article
- Mutations in the Transmembrane Domain and Cytoplasmic Tail of Hendra Virus Fusion Protein Disrupt Virus-Like-Particle Assembly.Journal of virology · 2017Article
- Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly.PLoS pathogens · 2015Article
- Human Metapneumovirus Is Capable of Entering Cells by Fusion with Endosomal Membranes.PLoS pathogens · 2015Article
- Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host.PloS one · 2015Article
- Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Viruses · 2014Review
- Biochemical, conformational, and immunogenic analysis of soluble trimeric forms of henipavirus fusion glycoproteins.Journal of virology · 2012Article
- Role of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.The Journal of biological chemistry · 2012Article
- Residues in the hendra virus fusion protein transmembrane domain are critical for endocytic recycling.Journal of virology · 2012Article
- Beyond anchoring: the expanding role of the hendra virus fusion protein transmembrane domain in protein folding, stability, and function.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Hendra virus fusion (F) protein is synthesized as a precursor protein, F(0), which is proteolytically processed to the mature form, F(1) + F(2). Unlike the case for the majority of paramyxovirus F proteins, the processing event is furin independent, does not require the addition of exogenous proteases, is not affected by reductions in intracellular Ca(2+), and is strongly affected by conditions that raise the intracellular pH (C. T. Pager, M. A. Wurth, and R. E. Dutch, J. Virol. 78:9154-9163, 2004). The Hendra virus F protein cytoplasmic tail contains a consensus motif for endocytosis, YXXPhi. To analyze the potential role of endocytosis in the processing and membrane fusion promotion of the Hendra virus F protein, mutation of tyrosine 525 to alanine (Hendra virus F Y525A) or phenylalanine (Hendra virus F Y525F) was performed. The rate of endocytosis of Hendra virus F Y525A was significantly reduced compared to that of the wild-type (wt) F protein, confirming the functional importance of the endocytosis motif. An intermediate level of endocytosis was observed for Hendra virus F Y525F. Surprisingly, dramatic reductions in the rate of proteolytic processing were observed for Hendra virus F Y525A, although initial transport to the cell surface was not affected. The levels of surface expression for both Hendra virus F Y525A and Hendra virus F Y525F were higher than that of the wt protein, and these mutants displayed enhanced syncytium formation. These results suggest that endocytosis is critically important for Hendra virus F protein cleavage, representing a new paradigm for proteolytic processing of paramyxovirus F proteins.
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Registered trials
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.