ArticleVeterinary research2021
Identification of a new amino acid mutation in the HN protein of NDV involved in pathogenicity.
Article in Veterinary research, 2021. 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, 12 citations in OpenAlex.
- Sialic acid biophore directed design of enhanced affinity HN protein from Newcastle disease virus.The FEBS journal · 2026Article
- Article
- The P protein T25M substitution is involved in the quasispecies and virulence of Newcastle disease virus.Microbiology spectrum · 2026Article
- Field outbreak investigation and immunoinformatic analysis suggest potential immune evasion by Newcastle disease virus Sub-Genotype XIV.2 in Nigeria.Scientific reports · 2025Article
- A novel pigeon paramyxovirus type 1 isolated from a sick racing pigeon in the Qinghai-Tibet Plateau of China shows high virulence in chickens.Veterinarni medicina · 2024Article
- Prevalence and Molecular Characterization of Bovine Parainfluenza Virus Type 3 in Cattle Herds in China.Animals : an open access journal from MDPI · 2023Article
- Article
- First Isolation and Characteristics of Bovine Parainfluenza Virus Type 3 from Yaks.Pathogens (Basel, Switzerland) · 2022Article
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
The fusion (F) and haemagglutinin-neuraminidase (HN) proteins of Newcastle disease virus (NDV) are viral entry proteins and are recognized as the major virulence determinants. Previously, a lentogenic NDV virus (CE16) was derived from a mesogenic strain (CI10) through sequential passages in chick embryos. Whole-genome sequence analysis revealed that the two homologous strains shared the same F protein but differed in HN with two amino acid (aa) substitutions (A215G and T430A). To elucidate the molecular reasons for virulence attenuation, two original plasmids (HN-CI10 and HN-CE16) and two single-point mutants (G215A and A430T) reverse-mutated from HN-CE16 were constructed to analyse the known biological functions of HN. The results showed that the A430T substitution significantly weakened the haemadsorption (HAd) activity, increased the neuraminidase (NA) activity, improved the fusion-promoting activity, and enhanced the cleavage-promoting activity of HN-CE16. However, G215A failed to induce obvious functional changes. Therefore, the aa residue HN430 may play a key role in determining virulence. To test this hypothesis, further studies on A430T were conducted through reverse genetics using an infectious cDNA clone. At the viral level, the A430T-mutated virus showed dramatic promotion of viral plaque formation, propagation, and pathogenicity in vitro and in vivo. This study demonstrates a new virulence site associated with HN protein functions, viral propagation, and pathogenicity. All these findings could lay a foundation for illuminating the molecular mechanism of NDV virulence.
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