[Expression and purification of heptad repeat region of the mumps virus F protein and analysis of characteristics].
Two Heptad repeat motifs (HR1 and HR2) from paramyxoviruses F protein could form thermostable heterodimers containing high alpha-helix while virus infected host cell. Following that the viral membrane and the host cell membrane were juxtaposed, which leads to membrane fusion. Mumps virus (MuV) is a member of the genus Rubulavirus in the family of Paramyxoviridae. MuV could use similar infection mechanism as well as other paramyxoviruses. In this study the HR1 and HR2 regions of MuV F protein were predicted by a computer program and expressed in E. coli with the GST fusion expression system. The GST fusion or GST-removed proteins were purified with Gluthathion Sepharose 4B Column. GST pull-down experiment suggested the interaction of HR1 and HR2 peptides, and analysis of gel filtration showed two peptides could form multimer, which indicates that the HR regions of MuV F protein may play an important role in virus fusion.
Liu
Yue-Yong
YY
Institute of Microbiology, College of Life Science, Zhejiang University, Hangzhou 310029, China.
Feng
Ming-Guang
MG
Zhu
Jie-Qing
JQ
Jiang
Li-Jie
LJ
Tien
Po
P
D008561:Membrane Fusion / Q000235:genetics; D009109:Mumps virus / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D020449:Repetitive Sequences, Amino Acid; D014760:Viral Fusion Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification
D011993:Recombinant Fusion Proteins; D014760:Viral Fusion Proteins