期刊
CELL HOST & MICROBE
卷 4, 期 6, 页码 600-608出版社
CELL PRESS
DOI: 10.1016/j.chom.2008.10.012
关键词
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资金
- National Institute of Allergy and Infectious Diseases [R01-AI075647, R21-AI067931]
- Cancer Center Core Support
- NIH/NCI [P30-CA13330]
Alphaviruses infect cells via a low-pH -triggered membrane fusion reaction mediated by the class II virus fusion protein E1, an elongated molecule with three extramembrane domains (DI-III). E1 drives fusion by inserting its fusion peptide loop into the target membrane and refolding to a hairpin-like trimer in which DIII moves toward the target membrane and packs against the central trimer. Three-dimensional structures provide static pictures of prefusion and postfusion E1 but do not explain this transition. Using truncated forms of E1, we reconstituted a low-pH-dependent intermediate composed of trimers; of DIM. Unexpectedly, DIM trimers were stable in the absence of DIII. Once formed at a low pH, DI/II trimers efficiently and specifically bound recombinant DIII through a pH-independent reaction. Even in the absence of DIII, DIM trimers interacted to form hexagonal lattices and to cause membrane deformation and tubulation. These studies identify a prefusion intermediate in class II membrane fusion.
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