In contrast, the BM2 protein of lineages II and III was observed to be evolving at rates of 3.80 × 10 −3 and 3.46 × 10 −3 aas/st/yr, respectively, which were unexpectedly higher than those of the HA protein.

Influenza B virus contains four integral membrane proteins in its envelope. Of these, BM2 has recently been found to have ion channel activity and is considered to be a functional counterpart to influenza A virus M2, but the role of BM2 in the life cycle of influenza B virus remains unclear.

Mar 6, 2019 · Influenza A and B viruses cause seasonal flu epidemics. The M2 protein of influenza B (BM2) is a membrane-embedded tetrameric proton channel that is essential for the viral lifecycle. BM2 is a...

Feb 3, 2020 · Here we report 1.4- and 1.5-Å solid-state NMR structures of the transmembrane domain of the closed and open BM2 channels in a phospholipid environment. Upon activation, the transmembrane helices...

Nov 8, 2009 · Influenza B virus contains an integral membrane protein, BM2, that oligomerizes in the viral membrane to form a pH-activated proton channel. Here we report the solution structures of both the...

Nov 1, 2016 · Flu A M2 protein (AM2) can be functionally replaced by that of Flu B (BM2). Both AM2 and BM2 with extended cytoplasmic tail are functional. Compatibility between the ion channel and the cytoplasmic tail is critical for M2 function. M2 with higher ion channel activity may augment influenza virus replication.

In the present study we have developed and optimized a robust strategy for the synthesis of highly hydrophobic peptides, especially membrane proteins, exemplarily using the influenza B M2 proton channel (BM2 (1–51)).

Mar 6, 2019 · Influenza A and B viruses cause seasonal flu epidemics. The M2 protein of influenza B (BM2) is a membrane-embedded tetrameric proton channel that is essential for the viral lifecycle. BM2 is a functional analog of AM2 but shares only 24% sequence identity for the transmembrane (TM) domain.

Jan 28, 2024 · The influenza BM2 transmembrane domain (BM2 TM), an acid-activated proton channel, is an attractive antiviral target due to its essential roles during influenza virus replication, whereas no effective inhibitors have been reported for BM2.

Feb 1, 2003 · The findings that BM2 and A/M2 anism, BM2 contains 109 residues and is oligomeric, have distinct TM domains that leads to largely protonmost likely a tetramer (Paterson et al., 2003), and the...