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

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....

Full description

Bibliographic Details
Main Authors: Julian Scherer, Richard B Vallee
Format: Article
Language:English
Published: MDPI AG 2011-08-01
Series:Viruses
Subjects:
Online Access:http://www.mdpi.com/1999-4915/3/8/1417/
_version_ 1818837137233018880
author Julian Scherer
Richard B Vallee
author_facet Julian Scherer
Richard B Vallee
author_sort Julian Scherer
collection DOAJ
description 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.
first_indexed 2024-12-19T03:17:43Z
format Article
id doaj.art-360b675c03cd4dc1aecd6f67e9b90391
institution Directory Open Access Journal
issn 1999-4915
language English
last_indexed 2024-12-19T03:17:43Z
publishDate 2011-08-01
publisher MDPI AG
record_format Article
series Viruses
spelling doaj.art-360b675c03cd4dc1aecd6f67e9b903912022-12-21T20:37:51ZengMDPI AGViruses1999-49152011-08-01381417143110.3390/v3081417Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed HexonJulian SchererRichard B ValleeFollowing 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.http://www.mdpi.com/1999-4915/3/8/1417/adenovirusmolecular motorscytoplasmic dyneinintracellular motility
spellingShingle Julian Scherer
Richard B Vallee
Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed Hexon
Viruses
adenovirus
molecular motors
cytoplasmic dynein
intracellular motility
title Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed Hexon
title_full Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed Hexon
title_fullStr Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed Hexon
title_full_unstemmed Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed Hexon
title_short Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed Hexon
title_sort adenovirus recruits dynein by an evolutionary novel mechanism involving direct binding to ph primed hexon
topic adenovirus
molecular motors
cytoplasmic dynein
intracellular motility
url http://www.mdpi.com/1999-4915/3/8/1417/
work_keys_str_mv AT julianscherer adenovirusrecruitsdyneinbyanevolutionarynovelmechanisminvolvingdirectbindingtophprimedhexon
AT richardbvallee adenovirusrecruitsdyneinbyanevolutionarynovelmechanisminvolvingdirectbindingtophprimedhexon