The fusion protein core of measles virus forms stable coiled-coil trimer.
Recent studies have shown that paramyxovirus might adopt a similar molecular mechanism of virus entry and fusion in which the attachment glycoprotein binds receptor/s and triggers the conformational changes of the fusion protein. There are two conserved regions of heptad repeat (HR1 and HR2) in the fusion protein and they were shown with fusion-inhibition effects in many paramyxoviruses, including measles virus. They also appear to show characteristic structure in the fusion core: the HR1/HR2 forms stable six-helix coiled-coil centered by HR1 and is surrounded by HR2 (trimer of HR1/HR2), which represents the post-fusion conformational structure. In this study, we expressed the HR1 and HR2 of measles virus fusion protein as a single chain (named 2-Helix) and subsequently tested its formation of trimer. Indeed, the results do show that the HR1 and HR2 interact with each other and form stable six-helix coiled-coil bundle. This is the first member in genus Morbillivirus of family Paramyxoviridae to be confirmed with this characteristic structure and provides the basis for the HR2-inhibition effects on virus fusion/entry for measles virus.
Zhu
Jieqing
J
Department of Molecular Virology, Institute of Microbiology, Chinese Academy of Sciences, Zhongguancun Beiyitiao, Beijing 100080, China.
Zhang
Catherine W-H
CW
Qi
Yipeng
Y
Tien
Po
P
Gao
George F
GF
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D008459:Measles virus / Q000737:chemistry* / Q000472:pathogenicity; D008561:Membrane Fusion; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D020449:Repetitive Sequences, Amino Acid; D016415:Sequence Alignment; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000378:metabolism
D014760:Viral Fusion Proteins