期刊
JOURNAL OF VIROLOGY
卷 87, 期 13, 页码 7558-7568出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00653-13
关键词
-
类别
资金
- U.S. Department of Energy, Office of Science
- Office of Basic Energy Sciences [W-31-109-Eng-38]
- Department of Energy
- Office of Biological and Environmental Research
- National Institutes of Health (NIH) [AI050066]
- National Center for Research Resources
- Biomedical Technology Program
- National Institute of General Medical Sciences
The phosphoprotein (P) is virally encoded by the Rhabdoviridae and Paramyxoviridae in the order Mononegavirales. P is a selfassociated oligomer and forms complexes with the large viral polymerase protein (L), the nucleocapsid protein (N), and the assembled nucleocapsid. P from different viruses has shown structural diversities even though their essential functions are the same. We systematically mapped the domains in mumps virus (MuV) P and investigated their interactions with nucleocapsidlike particles (NLPs). Similar to other P proteins, MuV P contains N-terminal, central, and C-terminal domains with flexible linkers between neighboring domains. By pulldown assays, we discovered that in addition to the previously proposed nucleocapsid binding domain (residues 343 to 391), the N-terminal region of MuV P (residues 1 to 194) could also bind NLPs. Further analysis of binding kinetics was conducted using surface plasmon resonance. This is the first observation that both the N-and C-terminal regions of a negative-strand RNA virus P are involved in binding the nucleocapsid. In addition, we defined the oligomerization domain (P-OD) of MuV P as residues 213 to 277 and determined its crystal structure. The tetrameric MuV P-OD is formed by one pair of long parallel alpha-helices with another pair in opposite orientation. Unlike the parallel orientation of each alpha-helix in the tetramer of Sendai virus P-OD, this represents a novel orientation of a P-OD where both the N-and the C-terminal domains are at either end of the tetramer. This is consistent with the observation that both the N-and the C-terminal domains are involved in binding the nucleocapsid.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据