期刊
JOURNAL OF VIROLOGY
卷 85, 期 18, 页码 9327-9333出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.05015-11
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资金
- Duke-NUS [R913-200-039-263]
- Western Regional Center of Excellence for Biodefense and Emerging Infectious Disease Research
- National Institutes of Health (NIH) [U54 AIO57156, P41RR002250]
Barmah Forest virus (BFV) is a mosquito-borne alphavirus that infects humans. A 6-angstrom-resolution cryo-electron microscopy three-dimensional structure of BFV exhibits a typical alphavirus organization, with RNA-containing nucleocapsid surrounded by a bilipid membrane anchored with the surface proteins E1 and E2. The map allows details of the transmembrane regions of E1 and E2 to be seen. The C-terminal end of the E2 transmembrane helix binds to the capsid protein. Following the E2 transmembrane helix, a short alpha-helical endodomain lies on the inner surface of the lipid envelope. The E2 endodomain interacts with E1 transmembrane helix from a neighboring E1-E2 trimeric spike, thereby acting as a spacer and a linker between spikes. In agreement with previous mutagenesis studies, the endodomain plays an important role in recruiting other E1-E2 spikes to the budding site during virus assembly. The E2 endodomain may thus serve as a target for antiviral drug design.
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