ArticleVirology journal2017
Two mutations in the HR2 region of Newcastle disease virus fusion protein with a cleavage motif "RRQRRL" are critical for fusogenic activity.
Article in Virology journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers, 1 of them a synthesis that pooled it.
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Who cites it
7 citing papers in PubMed, 1 synthesis or guideline pooled it, 11 citations in OpenAlex.
- Insights into the multifunctionality of viral glycoproteins F and HN in the lifecycle and pathogenesis of Newcastle disease virus: a systematic review.Veterinary research · 2025Pooled it
- A universal design of restructured dimer antigens: Development of a superior vaccine against the paramyxovirus in transgenic rice.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Genetic diversity of Newcastle disease viruses circulating in wild and synanthropic birds in Ukraine between 2006 and 2015.Frontiers in veterinary science · 2023Article
- Fusion Protein Cleavage Site Containing Three Basic Amino Acids Attenuates Newcastle Disease Virus in Chicken Embryos: Use as anFrontiers in microbiology · 2022Article
- Optimization of oncolytic effect of Newcastle disease virus Clone30 by selecting sensitive tumor host and constructing more oncolytic viruses.Gene therapy · 2021Article
- AvianFrontiers in veterinary science · 2021Review
- MiR-375 Has Contrasting Effects on Newcastle Disease Virus Growth Depending on the Target Gene.International journal of biological sciences · 2019Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundNewcastle disease virus (NDV) causes severe diseases in avian species. Its fusion protein cleavage site (Fcs) is a major contributor to virulence and membrane fusion. Previous studies showed that a change from phenylalanine (F) to lysine (L) at position 117 of the virulent strain fusion protein, which has the polybasic amino acid Fcs motif "
resultsThe exchanged regions between the fusion proteins of two strains, F48E9 and LaSota, showed that the region from amino acid 118-499 plays an important role in modulation of fusogenic activity in transfected cells. Further dissection of this region indicated that replacement of two amino acids (N479D, R486S) in heptad repeat 2 (HR2) of the avirulent fusion protein by the virulent counterpart resulted in fusion promotion. Moreover, the role of these two amino acids in fusion is dependent on the unique Fcs sequence "RRQRR↓L".
conclusionsOur results demonstrated that two amino acids (D479, S486) of the virulent strain F protein with this unique Fcs were critical for promoting fusogenic activity, and residue F or L at position 117 did not affect syncytium formation. These findings provide novel insights into fusogenic triggering by the fusion protein and may be useful for designing antiviral peptides.
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