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A Review of Functional Motifs Utilized by Viruses
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, in...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5217368/ https://www.ncbi.nlm.nih.gov/pubmed/28248213 http://dx.doi.org/10.3390/proteomes4010003 |
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author | Sobhy, Haitham |
author_facet | Sobhy, Haitham |
author_sort | Sobhy, Haitham |
collection | PubMed |
description | 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). |
format | Online Article Text |
id | pubmed-5217368 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-52173682017-02-27 A Review of Functional Motifs Utilized by Viruses Sobhy, Haitham Proteomes Review 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). MDPI 2016-01-21 /pmc/articles/PMC5217368/ /pubmed/28248213 http://dx.doi.org/10.3390/proteomes4010003 Text en © 2016 by the author; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Sobhy, Haitham A Review of Functional Motifs Utilized by Viruses |
title | A Review of Functional Motifs Utilized by Viruses |
title_full | A Review of Functional Motifs Utilized by Viruses |
title_fullStr | A Review of Functional Motifs Utilized by Viruses |
title_full_unstemmed | A Review of Functional Motifs Utilized by Viruses |
title_short | A Review of Functional Motifs Utilized by Viruses |
title_sort | review of functional motifs utilized by viruses |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5217368/ https://www.ncbi.nlm.nih.gov/pubmed/28248213 http://dx.doi.org/10.3390/proteomes4010003 |
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