Wicker Jason A, Whiteman Melissa C, Beasley David W C, Davis C Todd, Zhang Shuliu, Schneider Bradley S, Higgs Stephen, Kinney Richard M, Barrett Alan D T
Department of Microbiology and Immunology, Sealy Center for Vaccine Development, Center for Biodefense and Emerging Infectious Diseases, and Institute for Human Infections and Immunity, University of Texas Medical Branch at Galveston, TX 77555-0609, USA.
Virology. 2006 Jun 5;349(2):245-53. doi: 10.1016/j.virol.2006.03.007. Epub 2006 Apr 19.
West Nile virus (WNV) NS4B is a small hydrophobic nonstructural protein that is hypothesized to participate both in viral replication and evasion of host innate immune defenses. The protein has four cysteine residues (residues 102, 120, 227, and 237). Since cysteines are often critical for the function of proteins, each of the four cysteine residues found in WNV NS4B was mutated to serine by site-directed mutagenesis. While three of these substitutions had little effect on replication or mouse virulence phenotypes, the C102S mutation was associated with a temperature-sensitive phenotype at 41 degrees C as well as attenuation of the neuroinvasive and neurovirulence phenotypes in mice.
西尼罗河病毒(WNV)NS4B是一种小的疏水非结构蛋白,据推测它既参与病毒复制,又参与逃避宿主先天免疫防御。该蛋白有四个半胱氨酸残基(第102、120、227和237位残基)。由于半胱氨酸通常对蛋白质功能至关重要,通过定点诱变将WNV NS4B中发现的四个半胱氨酸残基中的每一个都突变为丝氨酸。虽然这些替代中的三个对复制或小鼠毒力表型影响不大,但C102S突变与41摄氏度时的温度敏感表型以及小鼠神经侵袭性和神经毒力表型的减弱有关。