影响莫洛尼鼠白血病病毒衣壳蛋白C末端部分的突变导致病毒体产生缺陷。
Defects in virion production caused by mutations affecting the C-terminal portion of the Moloney murine leukemia virus capsid protein.
作者信息
Wang Margaret Q, Goff Stephen P
机构信息
Department of Microbiology, Howard Hughes Medical Institute, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA.
出版信息
J Virol. 2003 Mar;77(5):3339-44. doi: 10.1128/jvi.77.5.3339-3344.2003.
Abstract
The capsid (CA) domain of the Moloney murine leukemia virus (Mo-MuLV) Gag protein has a unique carboxy terminus with a highly charged arginine-rich sequence. Mutant viruses harboring arginine-to-alanine mutations affecting this region of CA displayed significant defects in virion release, and the few viral particles produced were noninfectious. The interaction between the mutant Gag precursors was affected, as judged by the yeast two-hybrid assay. The results suggest that the unique carboxy terminus of CA in the Mo-MuLV plays an important role in Gag-Gag association during virion production.
摘要
莫洛尼鼠白血病病毒（Mo-MuLV）Gag蛋白的衣壳（CA）结构域具有独特的羧基末端，带有高度带电的富含精氨酸的序列。携带影响CA这一区域的精氨酸到丙氨酸突变的突变病毒在病毒粒子释放方面表现出显著缺陷，并且产生的少数病毒粒子没有感染性。通过酵母双杂交试验判断，突变Gag前体之间的相互作用受到了影响。结果表明，Mo-MuLV中CA独特的羧基末端在病毒粒子产生过程中的Gag-Gag缔合中起重要作用。
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