RT Journal Article SR Electronic(1) A1 Duan, Zhiqiang A1 Li, Juan A1 Zhu, Jie A1 Chen, Jian A1 Xu, Haixu A1 Wang, Yuyang A1 Liu, Huimou A1 Hu, Shunlin A1 Liu, XiufanYR 2014 T1 A single amino acid mutation, R42A, in the Newcastle disease virus matrix protein abrogates its nuclear localization and attenuates viral replication and pathogenicity JF Journal of General Virology, VO 95 IS 5 SP 1067 OP 1073 DO https://doi.org/10.1099/vir.0.062992-0 PB Microbiology Society, SN 1465-2099, AB 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.062992-0