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Proteomes 2016, 4(1), 3; doi:10.3390/proteomes4010003

A Review of Functional Motifs Utilized by Viruses

Department of Molecular Biology, Umeå University, 901 87 Umeå, Sweden
Academic Editor: Jacek R. Wisniewski
Received: 22 October 2015 / Revised: 7 January 2016 / Accepted: 13 January 2016 / Published: 21 January 2016
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Abstract

Short linear motifs (SLiM) are short peptides that facilitate protein function and protein-protein interactions. Viruses utilize these motifs to enter into the host, interact with cellular proteins, or egress from host cells. Studying functional motifs may help to predict protein characteristics, interactions, or the putative cellular role of a protein. In virology, it may reveal aspects of the virus tropism and help find antiviral therapeutics. This review highlights the recent understanding of functional motifs utilized by viruses. Special attention was paid to the function of proteins harboring these motifs, and viruses encoding these proteins. The review highlights motifs involved in (i) immune response and post-translational modifications (e.g., ubiquitylation, SUMOylation or ISGylation); (ii) virus-host cell interactions, including virus attachment, entry, fusion, egress and nuclear trafficking; (iii) virulence and antiviral activities; (iv) virion structure; and (v) low-complexity regions (LCRs) or motifs enriched with residues (Xaa-rich motifs). View Full-Text
Keywords: clathrin endocytosis; low-complexity repeats; ubiquitylation; agnoprotein; APOBEC; pentraxin; PDZ domain; retinoblastoma; inhibitor of apoptosis (IAP); transposition clathrin endocytosis; low-complexity repeats; ubiquitylation; agnoprotein; APOBEC; pentraxin; PDZ domain; retinoblastoma; inhibitor of apoptosis (IAP); transposition
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Sobhy, H. A Review of Functional Motifs Utilized by Viruses. Proteomes 2016, 4, 3.

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