Dynamic, but Not Necessarily Disordered, Human-Virus Interactions Mediated through SLiMs in Viral Proteins
Autor: | Jessica L. Gonzalez, Teresa Liberatore, Christian A. Balbin, Jessica Siltberg-Liberles, Heidy Elkhaligy |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
Proteome
viruses Amino Acid Motifs viral-host protein interaction Virulence Computational biology Review Biology Microbiology Genome Virus Viral Proteins Interaction network Virology Humans Short linear motif Protein Interaction Maps Databases Protein Virus classification intrinsically disordered protein regions the ELM database short eukaryotic linear motifs QR1-502 SLiMs Intrinsically Disordered Proteins Infectious Diseases Host-Pathogen Interactions Viruses Human Virus |
Zdroj: | Viruses Viruses, Vol 13, Iss 2369, p 2369 (2021) |
ISSN: | 1999-4915 |
Popis: | 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. |
Databáze: | OpenAIRE |
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