Please use this identifier to cite or link to this item: http://hdl.handle.net/10400.7/576
Title: Recycling Endosomes and Viral Infection
Author: Vale-Costa, Sílvia
Amorim, Maria
Keywords: animal viruses
intracellular membranes
recycling endosome
Rab GTPases
Rab11
phosphoinositides
Issue Date: 8-Mar-2016
Publisher: MDPI AG
Citation: Vale-Costa, S.; Amorim, M.J. Recycling Endosomes and Viral Infection. Viruses 2016, 8, 64.
Abstract: Many viruses exploit specific arms of the endomembrane system. The unique composition of each arm prompts the development of remarkably specific interactions between viruses and sub-organelles. This review focuses on the viral-host interactions occurring on the endocytic recycling compartment (ERC), and mediated by its regulatory Ras-related in brain (Rab) GTPase Rab11. This protein regulates trafficking from the ERC and the trans-Golgi network to the plasma membrane. Such transport comprises intricate networks of proteins/lipids operating sequentially from the membrane of origin up to the cell surface. Rab11 is also emerging as a critical factor in an increasing number of infections by major animal viruses, including pathogens that provoke human disease. Understanding the interplay between the ERC and viruses is a milestone in human health. Rab11 has been associated with several steps of the viral lifecycles by unclear processes that use sophisticated diversified host machinery. For this reason, we first explore the state-of-the-art on processes regulating membrane composition and trafficking. Subsequently, this review outlines viral interactions with the ERC, highlighting current knowledge on viral-host binding partners. Finally, using examples from the few mechanistic studies available we emphasize how ERC functions are adjusted during infection to remodel cytoskeleton dynamics, innate immunity and membrane composition.
Peer review: yes
URI: http://hdl.handle.net/10400.7/576
DOI: 10.3390/v8030064
Publisher Version: http://www.mdpi.com/1999-4915/8/3/64
Appears in Collections:CBVI- Artigos

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