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Respiratory syncytial virus uses a Vps4-independent budding mechanism controlled by Rab11-FIP2.


ABSTRACT: Respiratory syncytial virus (RSV) infects polarized epithelia, which have tightly regulated trafficking because of the separation and maintenance of the apical and basolateral membranes. Previously we established a link between the apical recycling endosome (ARE) and the assembly of RSV. The current studies tested the role of a major ARE-associated protein, Rab11 family interacting protein 2 (FIP2) in the virus life cycle. A dominant-negative form of FIP2 lacking its N-terminal C2 domain reduced the supernatant-associated RSV titer 1,000-fold and also caused the cell-associated virus titer to increase. These data suggested that the FIP2 C2 mutant caused a failure at the final budding step in the virus life cycle. Additionally, truncation of the Rab-binding domain from FIP2 caused its accumulation into mature filamentous virions. RSV budding was independent of the ESCRT machinery, the only well-defined budding mechanism for enveloped RNA viruses. Therefore, RSV uses a virus budding mechanism that is controlled by FIP2.

SUBMITTER: Utley TJ 

PROVIDER: S-EPMC2481327 | biostudies-other | 2008 Jul

REPOSITORIES: biostudies-other

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Respiratory syncytial virus uses a Vps4-independent budding mechanism controlled by Rab11-FIP2.

Utley Thomas J TJ   Ducharme Nicole A NA   Varthakavi Vasundhara V   Shepherd Bryan E BE   Santangelo Philip J PJ   Lindquist Michael E ME   Goldenring James R JR   Crowe James E JE  

Proceedings of the National Academy of Sciences of the United States of America 20080709 29


Respiratory syncytial virus (RSV) infects polarized epithelia, which have tightly regulated trafficking because of the separation and maintenance of the apical and basolateral membranes. Previously we established a link between the apical recycling endosome (ARE) and the assembly of RSV. The current studies tested the role of a major ARE-associated protein, Rab11 family interacting protein 2 (FIP2) in the virus life cycle. A dominant-negative form of FIP2 lacking its N-terminal C2 domain reduced  ...[more]

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