ArticleScientific reports2015
Two single amino acid substitutions in the intervening region of Newcastle disease virus HN protein attenuate viral replication and pathogenicity.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 23 citations in OpenAlex.
- Sialic acid biophore directed design of enhanced affinity HN protein from Newcastle disease virus.The FEBS journal · 2026Article
- Genotype IX Newcastle disease virus isolated from wild birds is attenuated by hemagglutinin-neuraminidase mutation.Journal of virology · 2026Article
- Prevalence, molecular characterization and phylogenetic analysis of Newcastle disease virus isolated from domestic poultry during 2019-2024 in Egypt.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Nucleotide sequence characterization, amino acid variations and 3D structural analysis of HN protein of the NDV VIId genotype.Veterinary medicine and science · 2024Article
- Phylogenetic Analysis of Newcastle Disease Virus Isolated from Poultry in Live Bird Markets and Wild Waterfowl in Zambia.Microorganisms · 2024Article
- Molecular evaluation and genetic characterisation of Newcastle disease virus's haemagglutinin-neuraminidase protein isolated from broiler chickens in Iran.Veterinary medicine and science · 2022Article
- Identification of a new amino acid mutation in the HN protein of NDV involved in pathogenicity.Veterinary research · 2021Article
- Application of Newcastle disease virus in the treatment of colorectal cancer.World journal of clinical cases · 2019Review
- Different Origins of Newcastle Disease Virus Hemagglutinin-Neuraminidase Protein Modulate the Replication Efficiency and Pathogenicity of the Virus.Frontiers in microbiology · 2017Article
- Contribution of HN protein length diversity to Newcastle disease virus virulence, replication and biological activities.Scientific reports · 2016Article
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6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Among the proteins encoded by Newcastle disease virus (NDV), the attachment protein (HN) is an important determinant of virulence and pathogenicity. HN has been molecularly characterized at the protein level; however, the relationship between the molecular character of HN and the animal pathotype it causes has not been well explored. Here, we revisited the intervening region (IR) of the HN stalk and extended the known biological functions of HN. Three distinct substitutions (A89Q, P93A, and L94A) in the IR of genotype VII NDV (G7 strain) HN protein were analyzed. The A89Q and L94A mutations weakened the fusion promotion activity of HN to 44% and 41% of that of wild type, respectively, whereas P93A decreased the neuraminidase activity to 21% of the parental level. At the virus level, P93A and L94A-bearing viruses displayed impaired receptor recognition ability, neuraminidase activity, and fusion-promoting activity, all of which led to virus attenuation. In addition, the L94A-mutated virus showed a dramatic decline in replication and was attenuated in cells and in chickens. Our data demonstrate that the HN biological activities and functions modulated by these specific amino acids in the IR are associated with NDV replication and pathogenicity.
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