Crystal Structure of the Oligomeric Form of Lassa Virus Matrix Protein Z

被引:26
作者
Hastie, Kathryn M. [1 ]
Zandonatti, Michelle [1 ]
Liu, Tong [2 ,4 ]
Li, Sheng [2 ]
Woods, Virgil L., Jr. [2 ]
Saphire, Erica Ollmann [1 ,3 ]
机构
[1] Scripps Res Inst, Dept Immunol & Microbial Sci, La Jolla, CA 92037 USA
[2] Univ Calif San Diego, Dept Med, La Jolla, CA 92093 USA
[3] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA
[4] Sequenom, San Diego, CA USA
基金
美国国家卫生研究院;
关键词
LYMPHOCYTIC CHORIOMENINGITIS VIRUS; ARENAVIRUS Z PROTEIN; MASS-SPECTROMETRY; RING; REVEALS; VP40; TRANSLATION; EXCHANGE; PML;
D O I
10.1128/JVI.02896-15
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The arenavirus matrix protein Z is highly multifunctional and occurs in both monomeric and oligomeric forms. The crystal structure of a dodecamer of Z from Lassa virus, presented here, illustrates a ring-like structure with a highly basic center. Mutagenesis demonstrates that the dimeric interface within the dodecamer and a Lys-Trp-Lys triad at the center of the ring are important for oligomerization. This structure provides an additional template to explore the many functions of Z.
引用
收藏
页码:4556 / 4562
页数:7
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