Viruses go modular

Viruses go modular
Title:
Viruses go modular
Other Titles:
Journal of Biological Chemistry
Publication Date:
28 February 2020
Citation:
J. Biol. Chem. 2020 295: 4604-. doi:10.1074/jbc.REV119.012414
Abstract:
The WW domain is a modular protein structure that recognizes the proline-rich Pro–Pro-x-Tyr (PPxY) motif contained in specific target proteins. The compact modular nature of the WW domain makes it ideal for mediating interactions between proteins in complex networks and signaling pathways of the cell (e.g. the Hippo pathway). As a result, WW domains play key roles in a plethora of both normal and disease processes. Intriguingly, RNA and DNA viruses have evolved strategies to hijack cellular WW domain–containing proteins and thereby exploit the modular functions of these host proteins for various steps of the virus lifecycle, including entry, replication, and egress. In this review, we summarize key findings in this rapidly expanding field, in which new virus–host interactions continue to be identified. Further unraveling of the molecular aspects of these crucial virus–host interactions will continue to enhance our fundamental understanding of the biology and pathogenesis of these viruses. We anticipate that additional insights into these interactions will help support strategies to develop a new class of small-molecule inhibitors of viral PPxY–host WW domain interactions that could be used as antiviral therapeutics.
License type:
PublisherCopyrights
Funding Info:
This work was supported in part by NIH grants AI102104, AI138052, AI138630, AI139392 and a University Research Foundation (URF) award to R.N.H., by internal grants from The National University of Singapore (R-185-000-2710-133 & 733) and the Mechanobiology Institute (R-714-018-006-271) to M.S., and by The Biomedical Research Council of A*STAR to H.F.
Description:
ISSN:
0021-9258
1083-351X
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