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Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed Hexon

Department of Pathology and Cell Biology, Columbia University, Physicians and Surgeons Building, Room 15-409, 630 West 168th Street, New York, NY 10032, USA
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Viruses 2011, 3(8), 1417-1431; https://doi.org/10.3390/v3081417
Received: 19 July 2011 / Revised: 3 August 2011 / Accepted: 6 August 2011 / Published: 12 August 2011
(This article belongs to the Special Issue Cytoskeleton in Viral Infections)
Following receptor-mediated uptake into endocytic vesicles and escape from the endosome, adenovirus is transported by cytoplasmic dynein along microtubules to the perinuclear region of the cell. How motor proteins are recruited to viruses for their own use has begun to be investigated only recently. We review here the evidence for a role for dynein and other motor proteins in adenovirus infectivity. We also discuss the implications of recent studies on the mechanism of dynein recruitment to adenovirus for understanding the relationship between pathogenic and physiological cargo recruitment and for the evolutionary origins of dynein-mediated adenovirus transport.
Keywords: adenovirus; molecular motors; cytoplasmic dynein; intracellular motility adenovirus; molecular motors; cytoplasmic dynein; intracellular motility
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MDPI and ACS Style

Scherer, J.; Vallee, R.B. Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed Hexon. Viruses 2011, 3, 1417-1431.

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