This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Martínez-Gil, L.
Right arrow Articles by Mingarro, I.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Martínez-Gil, L.
Right arrow Articles by Mingarro, I.

 Previous Article  |  Next Article 

Journal of Virology, June 2009, p. 5535-5543, Vol. 83, No. 11
0022-538X/09/$08.00+0     doi:10.1128/JVI.00393-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Plant Virus Cell-to-Cell Movement Is Not Dependent on the Transmembrane Disposition of Its Movement Protein{triangledown} ,{dagger}

Luis Martínez-Gil,1 Jesús A. Sánchez-Navarro,2 Antonio Cruz,3 Vicente Pallás,2 Jesús Pérez-Gil,3 and Ismael Mingarro1*

Departament de Bioquímica i Biologia Molecular, Universitat de València, E-46 100 Burjassot, Spain,1 Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-CSIC, E-46022 Valencia, Spain,2 Departamento de Bioquímica y Biología Molecular I, Universidad Complutense Madrid, E-28040 Madrid, Spain3

Received 23 February 2009/ Accepted 17 March 2009

The cell-to-cell transport of plant viruses depends on one or more virus-encoded movement proteins (MPs). Some MPs are integral membrane proteins that interact with the membrane of the endoplasmic reticulum, but a detailed understanding of the interaction between MPs and biological membranes has been lacking. The cell-to-cell movement of the Prunus necrotic ringspot virus (PNRSV) is facilitated by a single MP of the 30K superfamily. Here, using a myriad of biochemical and biophysical approaches, we show that the PNRSV MP contains only one hydrophobic region (HR) that interacts with the membrane interface, as opposed to being a transmembrane protein. We also show that a proline residue located in the middle of the HR constrains the structural conformation of this region at the membrane interface, and its replacement precludes virus movement.


* Corresponding author. Mailing address: Departament de Bioquímica i Biologia Molecular, Universitat de València, E-46 100 Burjassot, Spain. Phone: 34-963543796. Fax: 34-963544635. E-mail: Ismael.Mingarro{at}uv.es

{triangledown} Published ahead of print on 25 March 2009.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.


Journal of Virology, June 2009, p. 5535-5543, Vol. 83, No. 11
0022-538X/09/$08.00+0     doi:10.1128/JVI.00393-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.