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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-49285

Burckhardt, C J; Suomalainen, M; Schoenenberger, P; Boucke, K; Hemmi, S; Greber, U F (2011). Drifting Motions of the Adenovirus Receptor CAR and Immobile Integrins Initiate Virus Uncoating and Membrane Lytic Protein Exposure. Cell Host & Microbe, 10(2):105-117.

Accepted Version (English)


Viral particle binding to plasma membrane receptors elicits virus motions, recruits signaling proteins, and triggers membrane bending and fission, finally resulting in endocytic virus uptake. Here we analyze how human adenovirus engages its receptor coxsackievirus adenovirus receptor (CAR) and coreceptor αv integrin to move on the plasma membrane. Virus binding to CAR through fiber knobs gave rise to diffusive motions and actomyosin-2-dependent drifts, while integrin-targeted viruses were spatially more confined. Diffusions, drifts, and confined motions were specifically observed with viral particles that were subsequently internalized. CAR-mediated drifts together with integrin binding supported fiber shedding from adenovirus particles, leading to exposure of the membrane-lytic internal virion protein VI and enhanced viral escape from endosomes. Our results show that adenovirus uncoating is initiated at the plasma membrane by CAR drifting motion and binding to immobile integrins.

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Institute of Molecular Life Sciences
Special Collections > SystemsX.ch
Special Collections > SystemsX.ch > Research, Technology and Development Projects > LipidX
DDC:570 Life sciences; biology
Uncontrolled Keywords:CAR (Coxsackievirus Adenovirus Receptor); plasma membrane; infection; virus entry; trajectory segmentation; single particle tracking; actin; myosin-2; integrin; membrane penetration; movement; diffusion; surfing; confinement; motions
Deposited On:06 Sep 2011 13:43
Last Modified:27 Nov 2013 16:43
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1016/j.chom.2011.07.006
PubMed ID:21843868
Citations:Web of Science®. Times Cited: 34
Google Scholar™
Scopus®. Citation Count: 34

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