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Review

Dynamic, but Not Necessarily Disordered, Human-Virus Interactions Mediated through SLiMs in Viral Proteins

1
Department of Biological Sciences, Florida International University, Miami, FL 33199, USA
2
Biomolecular Sciences Institute, Florida International University, Miami, FL 33199, USA
*
Author to whom correspondence should be addressed.
Academic Editors: Parikshit Bagchi and Anupam Mukherjee
Viruses 2021, 13(12), 2369; https://doi.org/10.3390/v13122369
Received: 31 October 2021 / Revised: 15 November 2021 / Accepted: 16 November 2021 / Published: 26 November 2021
(This article belongs to the Special Issue Host Cell-Virus Interaction)
Most viruses have small genomes that encode proteins needed to perform essential enzymatic functions. Across virus families, primary enzyme functions are under functional constraint; however, secondary functions mediated by exposed protein surfaces that promote interactions with the host proteins may be less constrained. Viruses often form transient interactions with host proteins through conformationally flexible interfaces. Exposed flexible amino acid residues are known to evolve rapidly suggesting that secondary functions may generate diverse interaction potentials between viruses within the same viral family. One mechanism of interaction is viral mimicry through short linear motifs (SLiMs) that act as functional signatures in host proteins. Viral SLiMs display specific patterns of adjacent amino acids that resemble their host SLiMs and may occur by chance numerous times in viral proteins due to mutational and selective processes. Through mimicry of SLiMs in the host cell proteome, viruses can interfere with the protein interaction network of the host and utilize the host-cell machinery to their benefit. The overlap between rapidly evolving protein regions and the location of functionally critical SLiMs suggest that these motifs and their functional potential may be rapidly rewired causing variation in pathogenicity, infectivity, and virulence of related viruses. The following review provides an overview of known viral SLiMs with select examples of their role in the life cycle of a virus, and a discussion of the structural properties of experimentally validated SLiMs highlighting that a large portion of known viral SLiMs are devoid of predicted intrinsic disorder based on the viral SLiMs from the ELM database. View Full-Text
Keywords: short eukaryotic linear motifs; SLiMs; viral-host protein interaction; intrinsically disordered protein regions; the ELM database short eukaryotic linear motifs; SLiMs; viral-host protein interaction; intrinsically disordered protein regions; the ELM database
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MDPI and ACS Style

Elkhaligy, H.; Balbin, C.A.; Gonzalez, J.L.; Liberatore, T.; Siltberg-Liberles, J. Dynamic, but Not Necessarily Disordered, Human-Virus Interactions Mediated through SLiMs in Viral Proteins. Viruses 2021, 13, 2369. https://doi.org/10.3390/v13122369

AMA Style

Elkhaligy H, Balbin CA, Gonzalez JL, Liberatore T, Siltberg-Liberles J. Dynamic, but Not Necessarily Disordered, Human-Virus Interactions Mediated through SLiMs in Viral Proteins. Viruses. 2021; 13(12):2369. https://doi.org/10.3390/v13122369

Chicago/Turabian Style

Elkhaligy, Heidy, Christian A. Balbin, Jessica L. Gonzalez, Teresa Liberatore, and Jessica Siltberg-Liberles. 2021. "Dynamic, but Not Necessarily Disordered, Human-Virus Interactions Mediated through SLiMs in Viral Proteins" Viruses 13, no. 12: 2369. https://doi.org/10.3390/v13122369

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