Intramolecular complementation of measles virus fusion protein stability confers cell-cell fusion activity at 37 degree C

The fusion (F) protein of measles virus mediates membrane fusion. In this study, we investigated the molecular basis of the cell-cell fusion activity of the F protein. The N465H substitution in the heptad repeat B domain of the stalk region of the F protein eliminates this activity, but an additiona...

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Bibliographic Details
Published in:FEBS letters 2015-01, Vol.589 (1), p.152-158
Main Authors: Satoh, Yuto, Hirose, Mitsuhiro, Shogaki, Hiroko, Wakimoto, Hiroshi, Kitagawa, Yoshinori, Gotoh, Bin, Takahashi, Ken-ichi, Itoh, Masae
Format: Article
Language:English
Subjects:
Measles virus
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Summary:The fusion (F) protein of measles virus mediates membrane fusion. In this study, we investigated the molecular basis of the cell-cell fusion activity of the F protein. The N465H substitution in the heptad repeat B domain of the stalk region of the F protein eliminates this activity, but an additional mutation in the DIII domain of the head region - N183D, F217L, P219S, I225T or G240R - restores cell-cell fusion. Thermodynamically stabilized by the N465H substitution, the F protein required elevated temperature as high as 40 degree C to promote cell-cell fusion, whereas all five DIII mutations caused destabilization of the F protein allowing the highest fusion activity at 30 degree C. Stability complementation between the two domains conferred an efficient cell-cell fusion activity on the F protein at 37 degree C.
ISSN:0014-5793
DOI:10.1016/j.febslet.2014.11.040