tetano
Editor, Senior Moderator
Virology. 2016 Aug 24;498:99-108. doi: 10.1016/j.virol.2016.08.016. [Epub ahead of print]
[h=1]Influenza B virus M2 protein can functionally replace its influenza A virus counterpart in promoting virus replication.[/h] Wanitchang A[SUP]1[/SUP], Wongthida P[SUP]1[/SUP], Jongkaewwattana A[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The M2 protein (AM2 and BM2) of influenza A and B viruses function as a proton channel essential for viral replication. They also carry a cytoplasmic tail whose functions are not fully delineated. It is currently unknown whether these proteins could be replaced functionally in a viral context. Here, we generated single-cycle influenza A viruses (scIAV-ΔHA) carrying various M2-2A-mCherry constructs in the segment 4 (HA) and evaluated their growth in complementing cells. Intriguingly, the scIAV-ΔHA carrying AM2 and that bearing BM2 grew comparably well in MDCK-HA cells. Furthermore, while the virus carrying chimeric B-AM2 in which the BM2 transmembrane fused with the AM2 cytoplasmic tail produced robust infection, the one bearing the AM2 transmembrane fused with the BM2 cytoplasmic tail (A-BM2) exhibited severely impaired growth. Altogether, we demonstrate that AM2 and BM2 are functionally interchangeable and underscore the role of compatibility between transmembrane and cytoplasmic tail of the M2 protein.
Copyright ? 2016 Elsevier Inc. All rights reserved.
[h=4]KEYWORDS:[/h] AM2; BM2; Chimeric protein; Cytoplasmic tail; Proton channel; ScIAV-ΔHA
PMID: 27567258 DOI: 10.1016/j.virol.2016.08.016
[PubMed - as supplied by publisher]
[h=1]Influenza B virus M2 protein can functionally replace its influenza A virus counterpart in promoting virus replication.[/h] Wanitchang A[SUP]1[/SUP], Wongthida P[SUP]1[/SUP], Jongkaewwattana A[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The M2 protein (AM2 and BM2) of influenza A and B viruses function as a proton channel essential for viral replication. They also carry a cytoplasmic tail whose functions are not fully delineated. It is currently unknown whether these proteins could be replaced functionally in a viral context. Here, we generated single-cycle influenza A viruses (scIAV-ΔHA) carrying various M2-2A-mCherry constructs in the segment 4 (HA) and evaluated their growth in complementing cells. Intriguingly, the scIAV-ΔHA carrying AM2 and that bearing BM2 grew comparably well in MDCK-HA cells. Furthermore, while the virus carrying chimeric B-AM2 in which the BM2 transmembrane fused with the AM2 cytoplasmic tail produced robust infection, the one bearing the AM2 transmembrane fused with the BM2 cytoplasmic tail (A-BM2) exhibited severely impaired growth. Altogether, we demonstrate that AM2 and BM2 are functionally interchangeable and underscore the role of compatibility between transmembrane and cytoplasmic tail of the M2 protein.
Copyright ? 2016 Elsevier Inc. All rights reserved.
[h=4]KEYWORDS:[/h] AM2; BM2; Chimeric protein; Cytoplasmic tail; Proton channel; ScIAV-ΔHA
PMID: 27567258 DOI: 10.1016/j.virol.2016.08.016
[PubMed - as supplied by publisher]