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Interaction of influenza A virus matrix protein with RACK1 is required for virus release

: Demirov, D.; Gabriel, G.; Schneider, C.; Hohenberg, H.; Ludwig, S.


Cellular microbiology 14 (2012), No.5, pp.774-789
ISSN: 1462-5814
ISSN: 1462-5822
Journal Article
Fraunhofer IME ()

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 cro ss-talk with a RACK1-mediated pathway.