N-terminal domain of PB1-F2 protein of influenza A virus can fold into amyloid-like oligomers and damage cholesterol and cardiolipid containing membranes

Composition‐dependent membrane disruption by the proapoptotic protein PB1F2 from HK97 influenza A virus

“…Probes that are sensitive to the MMP, such as mito‐tracker, have been used to test the influence of PB1F2 on the MMP in vivo . Similarly, in vitro permeabilization tests can be carried out by monitoring liposome leakage, and this approach also confirmed the ability of PB1F2 to affect the MMP . The mitochondrial targeting of PB1F2 is mediated largely by the predicted helices in the C‐terminal region of the protein .…”

“…Fig. S1 shows the sequence alignment of the three most frequently studied PB1F2 variants derived from influenza A virus strains A/Puerto Rico/8/34 (H1N1) , A/Wilson‐Smith/1933 (H1N1) , and HK97 (Fig. S1).…”

“…PB1F2 was first identified as a membrane protein localized to mitochondria that induces cell death. Researchers have synthesized PB1F2 (PR8) and its fragments by solid‐phase peptide synthesis (SPS) methods, and investigated the biological functions of the peptides . Chevalier et al .…”

“…Researchers have synthesized PB1F2 (PR8) and its fragments by solid-phase peptide synthesis (SPS) methods, and investigated the biological functions of the peptides [16,17]. Chevalier et al [15] first reported the expression of PB1F2 in E. coli BL21 and subsequent purification by unfolding and refolding of insoluble inclusion bodies.…”

“…Moreover, PB1F2 has been reported to form protein channel pores with no appreciable ion selectivity for which the C terminus is necessary . PB1F2 was reported to be monomeric with random coiled structure at pH5 . PB1F2 protein can also adopt β‐sheet conformation in the membrane‐mimicking detergent or in the presence of liposomes.…”