tetano
Editor, Senior Moderator
Cell Microbiol. 2012 Jan 31. doi: 10.1111/j.1462-5822.2012.01759.x. [Epub ahead of print]
Interaction of influenza A virus matrix protein with RACK1 is required for virus release.
Demirov D, Gabriel G, Schneider C, Hohenberg H, Ludwig S.
Source
Institute of Molecular Virology (IMV), Centre for Molecular Biology of Inflammation (ZMBE), University of M?nster, 48149 M?nster, Germany Heinrich-Pette-Institute, Leibniz Institute for Experimental Virology, 20251 Hamburg, Germany.
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 crosstalk with a RACK1-mediated pathway. ? 2012 Blackwell Publishing Ltd.
? 2012 Blackwell Publishing Ltd.
PMID:
22289149
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22289149
Interaction of influenza A virus matrix protein with RACK1 is required for virus release.
Demirov D, Gabriel G, Schneider C, Hohenberg H, Ludwig S.
Source
Institute of Molecular Virology (IMV), Centre for Molecular Biology of Inflammation (ZMBE), University of M?nster, 48149 M?nster, Germany Heinrich-Pette-Institute, Leibniz Institute for Experimental Virology, 20251 Hamburg, Germany.
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 crosstalk with a RACK1-mediated pathway. ? 2012 Blackwell Publishing Ltd.
? 2012 Blackwell Publishing Ltd.
PMID:
22289149
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22289149