Project description:Newcastle Disease Virus (NDV) is one of the most threatening viruses to the poultry industry, and it also exhibits oncolytic properties. In our research, we identified a non-oncolytic strain, genotype VII NDV strain I4, where the lack of oncolytic ability is attributed to its NP protein. To explore the mechanism of NP-mediated oncolysis by NDV, we focused on the differential interacting proteins of the NP proteins from two strains: the highly oncolytic Herts/33 strain and the poorly oncolytic I4 strain. The mass spectrometry results show the interacting protein profiles of the NP proteins from both virus strains. After infecting HeLa cells with each strain, we conducted immunoprecipitation using antibodies against the NP protein. Due to the lower expression of I4-associated proteins during replication, we further performed immunoprecipitation experiments using separately overexpressed NP proteins from I4 and Herts/33.
Project description:Newcastle disease virus (NDV) is one of the most significant threats to the poultry industry, and it also exhibits oncolytic properties. In our research, we have identified a non-oncolytic strain, the genotype VII NDV strain I4. We have found that the lack of oncolytic characteristics in this strain is attributed to amino acids 366-489 in the NP protein. To delve into the mechanism of NP-mediated NDV oncolysis, we initiated further investigations using the highly oncolytic Herts/33 strain's NP and a recombinant NP protein with amino acids 366-489 from the I4 strain substituted in (H-NP366-489I). These proteins represent the interacting partners in the proteomics analysis of NP proteins from both viral strains. After infecting HeLa cells with each of these strains, immunoprecipitation was performed using antibodies targeting the NP protein. Since the H-NP366-489I virus produces fewer proteins during replication, we additionally overexpressed the H-NP366-489I and Herts/33 NP proteins separately for immunoprecipitation experiments.