Key result
Tulane virus NS1-2 functions as an enteric calicivirus viroporin that induces aberrant cellular calcium signaling to facilitate virus replication.
Why the study?
Mechanistic insights into the viral factors and host pathways important for enteric calicivirus replication and infection are still largely lacking.
The identification of NS1-2 as a viroporin that mediates calcium signaling for enteric calicivirus replication provides a novel target for developing antivirals.
Viroporin blockade may warrant exploration as antiviral strategy; leaves open whether findings extend to human norovirus pathogenesis.
Tulane virus is one of many enteric caliciviruses that cause acute gastroenteritis and diarrheal disease. Globally, enteric caliciviruses affect both humans and animals and amass >65 billion dollars per year in treatment and health care-associated costs, thus imposing an enormous economic burden. Recent progress has resulted in several cultivation systems (B cells, enteroids, and zebrafish larvae) to study human noroviruses, but mechanistic insights into the viral factors and host pathways important for enteric calicivirus replication and infection are still largely lacking. Here, we used Tulane virus, a calicivirus that is biologically similar to human noroviruses and can be cultivated by conventional cell culture, to identify and functionally validate NS1-2 as an enteric calicivirus viroporin. Viroporin-mediated calcium signaling may be a broadly utilized pathway for enteric virus replication, and its existence within caliciviruses provides a novel approach to developing antivirals and comprehensive therapeutics for enteric calicivirus diarrheal disease outbreaks.
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Strtak et al. (2019) studied enteric calicivirus infection. Tulane virus NS1-2 was evaluated on Viroporin activity and calcium signaling. Tulane virus NS1-2 functions as an enteric calicivirus viroporin that induces aberrant cellular calcium signaling to facilitate virus replication.
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