Open AccessInteraction of influenza A virus matrix protein with RACK1 is required for virus release
Author(s) -
Demirov Dimiter,
Gabriel Gülsah,
Schneider Carola,
Hohenberg Heinrich,
Ludwig Stephan
Publication year - 2012
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/j.1462-5822.2012.01759.x
Subject(s) - vp40 , viral matrix protein , budding , virus , biology , influenza a virus , virology , proline , rna , microbiology and biotechnology , biochemistry , gene , amino acid
Summary 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.