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- Title
Interaction of influenza A virus matrix protein with RACK1 is required for virus release.
- Authors
Demirov, Dimiter; Gabriel, Gülsah; Schneider, Carola; Hohenberg, Heinrich; Ludwig, Stephan
- Abstract
The mechanism of budding of influenza A virus revealed important deviation from the consensus mechanism of budding of retroviruses and of a growing number of negative-strand RNA viruses. This study is focused on the role of the influenza A virus matrix protein M1 in virus release. We found that a mutation of the proline residue at position 16 of the matrix protein induces inhibition of virus detachment from cells. Depletion of the M1-binding protein RACK1 also impairs virus release and RACK1 binding requires the proline residue at position 16 of M1. The impaired M1-RACK1 interaction does not affect the plasma membrane binding of M1; in contrast, RACK1 is recruited to detergent-resistant membranes in a M1-proline-16-dependent manner. The proline-16 mutation in M1 and depletion of RACK1 impairs the pinching-off of the budding virus particles. These findings reveal the active role of the viral matrix protein in the release of influenza A virus particles that involves a cross-talk with a RACK1-mediated pathway.
- Publication
Cellular microbiology, 2012, Vol 14, Issue 5, p774
- ISSN
1462-5822
- Publication type
Journal Article
- DOI
10.1111/j.1462-5822.2012.01759.x