Residue Gln370 of Newcastle disease virus nucleoprotein mediate viral inclusion body-like structure formation via interaction with residue Ser254 of viral phosphoprotein
5 affiliations
- 1Poultry Institute, Shandong Academy of Agricultural Science, Jinan, China
- 2Jinan Key Laboratory for Agricultural Experimental Animal and Comparative Medicine, Jinan, China
- 3Shandong Provincial Key Laboratory of Livestock and Poultry Breeding (PKL2024B15), Shandong Academy of Agricultural Sciences, Jinan, China
- 4College of Veterinary Medicine, Northwest A&F University, Yangling, China
- 5Institute of Experimental Veterinary Medicine named of S.N. Vyshelessky, Minsk, Belarus
Abstract
BackgroundNewcastle disease virus (NDV) infects more than 250 avian species and mammals. Cytoplasmic inclusion bodies (IBs) are a hallmark of paramyxovirus infection; however, the molecular mechanisms underlying NDV IB formation remain poorly understood.MethodsIn this study, we investigated the interactive sites of viral protein driving IB-like structure formation via transmission electron microscopy, immunofluorescence assays (IFA), viral titration, co-immunoprecipitation (co-IP), structural modeling analysis.ResultsBoth virulent and attenuated NDV strains induced IBs in chicken-, mouse-, and human-derived cells. And the virus replicated well in CEF and HeLa cells rather than MEF. Time-course analysis revealed that IBs emerged as small puncta early in infection, increased in size over time, and ultimately accumulated in the perinuclear region. Co-immunoprecipitation (co-IP) and IFA revealed that amino acid residues 367–375 of the nucleoprotein (NP) bound to the PMD of the phosphoprotein (P), and this interaction was required for IB-like structure assembly. Furthermore, structural modeling and experiments of the NP–P complex identified residues Gln370 of NP and residue Ser254 of P as the principal contact and interacting sites for IB-like structure assembly.DiscussionThese findings reveal a previously unrecognized NP–P binding interface that mediates NDV IB formation, providing new insights into the molecular basis of viral condensate biogenesis in paramyxoviruses and a potential target for antiviral intervention.
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BibTeX
@article{wang2026residue,
title = {{Residue Gln370 of Newcastle disease virus nucleoprotein mediate viral inclusion body-like structure formation via interaction with residue Ser254 of viral phosphoprotein}},
author = {Wenbin Wang and Wenbin Wang and Wenbin Wang and Sa Xiao and Yuxia Zhang and Yuxia Zhang and Yuxia Zhang and Xiaoyuan Yuan and Xiaoyuan Yuan and Xiaoyuan Yuan and Wenwen Dong and Wenwen Dong and Wenwen Dong and Zhuoming Qin and Zhuoming Qin and Zhuoming Qin and Feng Hu and Feng Hu and Feng Hu and Kexiang Yu and Kexiang Yu and Kexiang Yu and Dzmitry Barysavets and Nasonau Ihar and Shchemialiova Natallia and Hongliang Wang and Guiming Li and Guiming Li and Guiming Li},
journal = {Frontiers in Cellular and Infection Microbiology},
year = {2026},
month = oct,
doi = {10.3389/fcimb.2026.1978310},
url = {https://doi.org/10.3389/fcimb.2026.1978310},
note = {CC BY},
}
RIS
TY - JOUR
TI - Residue Gln370 of Newcastle disease virus nucleoprotein mediate viral inclusion body-like structure formation via interaction with residue Ser254 of viral phosphoprotein
AU - Wenbin Wang
AU - Wenbin Wang
AU - Wenbin Wang
AU - Sa Xiao
AU - Yuxia Zhang
AU - Yuxia Zhang
AU - Yuxia Zhang
AU - Xiaoyuan Yuan
AU - Xiaoyuan Yuan
AU - Xiaoyuan Yuan
AU - Wenwen Dong
AU - Wenwen Dong
AU - Wenwen Dong
AU - Zhuoming Qin
AU - Zhuoming Qin
AU - Zhuoming Qin
AU - Feng Hu
AU - Feng Hu
AU - Feng Hu
AU - Kexiang Yu
AU - Kexiang Yu
AU - Kexiang Yu
AU - Dzmitry Barysavets
AU - Nasonau Ihar
AU - Shchemialiova Natallia
AU - Hongliang Wang
AU - Guiming Li
AU - Guiming Li
AU - Guiming Li
PY - 2026
DA - 2026/10/23
JO - Frontiers in Cellular and Infection Microbiology
DO - 10.3389/fcimb.2026.1978310
UR - https://doi.org/10.3389/fcimb.2026.1978310
AB - BackgroundNewcastle disease virus (NDV) infects more than 250 avian species and mammals. Cytoplasmic inclusion bodies (IBs) are a hallmark of paramyxovirus infection; however, the molecular mechanisms underlying NDV IB formation remain poorly understood.MethodsIn this study, we investigated the interactive sites of viral protein driving IB-like structure formation via transmission electron microscopy, immunofluorescence assays (IFA), viral titration, co-immunoprecipitation (co-IP), structural modeling analysis.ResultsBoth virulent and attenuated NDV strains induced IBs in chicken-, mouse-, and human-derived cells. And the virus replicated well in CEF and HeLa cells rather than MEF. Time-course analysis revealed that IBs emerged as small puncta early in infection, increased in size over time, and ultimately accumulated in the perinuclear region. Co-immunoprecipitation (co-IP) and IFA revealed that amino acid residues 367–375 of the nucleoprotein (NP) bound to the PMD of the phosphoprotein (P), and this interaction was required for IB-like structure assembly. Furthermore, structural modeling and experiments of the NP–P complex identified residues Gln370 of NP and residue Ser254 of P as the principal contact and interacting sites for IB-like structure assembly.DiscussionThese findings reveal a previously unrecognized NP–P binding interface that mediates NDV IB formation, providing new insights into the molecular basis of viral condensate biogenesis in paramyxoviruses and a potential target for antiviral intervention.
SN - 2235-2988
ER -