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Composition‐dependent membrane disruption by the proapoptotic protein PB 1F2 from HK 97 influenza A virus
Author(s) -
Wang Yujuan,
Yang Jing,
Wang Jiarong,
Zhu Lei,
Wang Junfeng
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13172
Subject(s) - membrane , inner mitochondrial membrane , chemistry , microbiology and biotechnology , lipid bilayer , mitochondrion , micelle , phosphatidylcholine , membrane protein , biology , biochemistry , phospholipid , aqueous solution
PB 1F2 is a proapoptotic protein encoded by an alternative reading frame in the influenza A virus. Its accumulation accelerates mitochondrial fragmentation by decreasing the mitochondrial membrane potential following translocation into the mitochondrial inner membrane space, but the mechanistic underpinnings remain unclear. Herein, the PB 1F2 from HK 97 was expressed and purified in soluble form. The interaction between PB 1F2 and the mitochondrial membrane were investigated using three membrane mimics, liposomes, bicelles, and nanodiscs. We show that the interactions between PB 1F2 and membrane mimics depend on lipid type and are time‐ and dose‐dependent. The primary membrane target of PB 1F2 is phosphatidylcholine, the lipid that forms the major component of mitochondrial inner membranes. PB 1F2 disrupts the integrity of lipid membranes by forming micelle‐like PB 1F2–lipid assemblies.