Molecular chaperone Hsp90 is a therapeutic target for noroviruses.
Surender VashistLuis UrenaMariam B Gonzalez-HernandezJayoung ChoiAlexis de RougemontJoana Rocha-PereiraJohan NeytsSeungmin HwangChristiane E WobusIan GoodfellowPublished in: Journal of virology (2015)
HuNoV are a major cause of acute gastroenteritis around the world. RNA viruses, including noroviruses, rely heavily on host cell proteins and pathways for all aspects of their life cycle. Here, we identify one such protein, the molecular chaperone Hsp90, as an important factor required during the norovirus life cycle. We demonstrate that both murine and human noroviruses require the activity of Hsp90 for the stability of their capsid proteins. Furthermore, we demonstrate that targeting Hsp90 activity in vivo using small molecule inhibitors also reduces infectious virus production. Given the considerable interest in the development of Hsp90 inhibitors for use in cancer therapeutics, we identify here a new target that could be explored for the development of antiviral strategies to control norovirus outbreaks and treat chronic norovirus infection in immunosuppressed patients.
Keyphrases
- heat shock protein
- life cycle
- heat shock
- small molecule
- heat stress
- end stage renal disease
- protein protein
- ejection fraction
- newly diagnosed
- endothelial cells
- liver failure
- peritoneal dialysis
- stem cells
- prognostic factors
- drug induced
- papillary thyroid
- oxidative stress
- squamous cell carcinoma
- single cell
- cancer therapy
- single molecule
- patient reported outcomes
- mesenchymal stem cells
- amino acid
- aortic dissection
- induced pluripotent stem cells
- nucleic acid