@article{mbs:/content/journal/jgv/10.1099/vir.0.062992-0, author = "Duan, Zhiqiang and Li, Juan and Zhu, Jie and Chen, Jian and Xu, Haixu and Wang, Yuyang and Liu, Huimou and Hu, Shunlin and Liu, Xiufan", title = "A single amino acid mutation, R42A, in the Newcastle disease virus matrix protein abrogates its nuclear localization and attenuates viral replication and pathogenicity", journal= "Journal of General Virology", year = "2014", volume = "95", number = "5", pages = "1067-1073", doi = "https://doi.org/10.1099/vir.0.062992-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.062992-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The Newcastle disease virus (NDV) matrix (M) protein is a highly basic and nucleocytoplasmic shuttling viral protein. Previous study has demonstrated that the N-terminal 100 aa of NDV M protein are somewhat acidic overall, but the remainder of the polypeptide is strongly basic. In this study, we investigated the role of the N-terminal basic residues in the subcellular localization of M protein and in the replication and pathogenicity of NDV. We found that mutation of the basic residue arginine (R) to alanine (A) at position 42 disrupted M’s nuclear localization. Moreover, a recombinant virus with R42A mutation in the M protein reduced viral replication in DF-1 cells and attenuated the virulence and pathogenicity of the virus in chickens. This is the first report to show that a basic residue mutation in the NDV M protein abrogates its nuclear localization and attenuates viral replication and pathogenicity.", }