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Targeting of MuLV Gag to the plasma membrane is mediated by PI(4,5)P2 and PhosphatidylSerine

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HAL Id: inserm-00649349

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Targeting of MuLV Gag to the plasma membrane is mediated by PI(4,5)P2 and PhosphatidylSerine

Elise Hamard-Peron, Franceline Juilliard, Js Saad, C Roy, Philippe Roingeard, Michael Summers, Jean-Luc Darlix, C. Picart, Delphine Muriaux

To cite this version:

Elise Hamard-Peron, Franceline Juilliard, Js Saad, C Roy, Philippe Roingeard, et al.. Targeting of

MuLV Gag to the plasma membrane is mediated by PI(4,5)P2 and PhosphatidylSerine. Retrovirology,

BioMed Central, 2009, 6 (Suppl 2), 6 (Suppl 2):O15. �10.1186/1742-4690-6-S2-O15�. �inserm-00649349�

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BioMed Central

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Retrovirology

Open Access

Oral presentation

Targeting of MuLV Gag to the plasma membrane is mediated by PI(4,5)P

2

and PhosphatidylSerine

E Hamard-Peron

1

, F Juilliard

1

, JS Saad

2,3

, C Roy

4

, P Roingeard

5

, Michael F Summers

2

, JL Darlix

1

, C Picart

4

and D Muriaux*

1,6

Address: 1LaboRetro, InsermU758, ENS de Lyon, IFR128, 69364 Lyon, France, 2Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, Maryland 21250, USA, 3Department of

Microbiology, University of Alabama at Birmingham, 845 19th street south, Birmingham, AL 35294, USA, 4CNRS-UMR 5235, Université de Montpellier 2, Montpellier, France, 5Inserm U966, Université François Rabelais, Tours, France and 6CNRS-UMR 5628, LMGP, 3 parvis L. Neel, 38016 Grenoble, France

* Corresponding author

Membrane targeting by the modern human immunodefi- ciency viruses is dependent on the plasma membrane- located phospholipid PI(4,5)P2. In order to determine if evolutionarily distant retroviruses are targeted by a similar mechanism, we generated mutant Gag constructs in the matrix (MA) domain of the Murine Leukemia Virus (MuLV) and examined their binding to membrane mod- els and phenotypes in cell culture. Mutations in the MA polybasic region altered Gag localization, membrane binding and virion production. In addition, we show that MA binds with good affinity to all the phosphatidylinosi- tol phosphates but displays a strong specificity for PI(4,5)P2 only if enhanced by phophatidylserine. Virus production was strongly impaired by PI(4,5)P2 depletion under 5ptaseIV overexpression. Our results suggest that the N-terminal polybasic region of MA is essential for Gag targeting to the plasma membrane and Gag cellular traf- ficking. The binding of the MA domain to PI(4,5)P2 appears to be a conserved feature among retroviruses, despite the fact that the MuLV-MA domain is structurally different from that of HIV-1 and -2 and lacks a readily identifiable PI(4,5)P2 binding cleft.

from Frontiers of Retrovirology: Complex retroviruses, retroelements and their hosts Montpellier, France. 21-23 September 2009

Published: 24 September 2009

Retrovirology 2009, 6(Suppl 2):O15 doi:10.1186/1742-4690-6-S2-O15

<supplement> <title> <p>Frontiers of Retrovirology: Complex retroviruses, retroelements and their hosts</p> </title> <note>Meeting abstracts - A single PDF containing all abstracts in this Supplement is available <a href="http://www.biomedcentral.com/content/files/pdf/1742-4690-6-S2-full.pdf">here</a>.</note> <url>http://www.biomedcentral.com/content/pdf/1742-4690-6-S2-info.pdf</url> </supplement>

This abstract is available from: http://www.retrovirology.com/content/6/S2/O15

© 2009 Hamard-Peron et al; licensee BioMed Central Ltd.

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