In silico analysis of functional single nucleotide polymorphisms in the human TRIM22 gene.

Tripartite motif protein 22 (TRIM22) is an evolutionarily ancient protein that plays an integral role in the host innate immune response to viruses. The antiviral TRIM22 protein has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 ex...

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Autores principales:	Jenna N Kelly, Stephen D Barr
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7bcda800c4f24e438fe945a80da6ee1d
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spelling	oai:doaj.org-article:7bcda800c4f24e438fe945a80da6ee1d2021-11-25T06:10:08ZIn silico analysis of functional single nucleotide polymorphisms in the human TRIM22 gene.1932-620310.1371/journal.pone.0101436https://doaj.org/article/7bcda800c4f24e438fe945a80da6ee1d2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24983760/?tool=EBIhttps://doaj.org/toc/1932-6203Tripartite motif protein 22 (TRIM22) is an evolutionarily ancient protein that plays an integral role in the host innate immune response to viruses. The antiviral TRIM22 protein has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. In this study, multiple in silico computational methods were used to identify non-synonymous or amino acid-changing SNPs (nsSNP) that are deleterious to TRIM22 structure and/or function. A sequence homology-based approach was adopted for screening nsSNPs in TRIM22, including six different in silico prediction algorithms and evolutionary conservation data from the ConSurf web server. In total, 14 high-risk nsSNPs were identified in TRIM22, most of which are located in a protein interaction module called the B30.2 domain. Additionally, 9 of the top high-risk nsSNPs altered the putative structure of TRIM22's B30.2 domain, particularly in the surface-exposed v2 and v3 regions. These same regions are critical for retroviral restriction by the closely-related TRIM5α protein. A number of putative structural and functional residues, including several sites that undergo post-translational modification, were also identified in TRIM22. This study is the first extensive in silico analysis of the highly polymorphic TRIM22 gene and will be a valuable resource for future targeted mechanistic and population-based studies.Jenna N KellyStephen D BarrPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 7, p e101436 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jenna N Kelly Stephen D Barr In silico analysis of functional single nucleotide polymorphisms in the human TRIM22 gene.
description	Tripartite motif protein 22 (TRIM22) is an evolutionarily ancient protein that plays an integral role in the host innate immune response to viruses. The antiviral TRIM22 protein has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 expression has also been associated with multiple sclerosis, cancer, and autoimmune disease. In this study, multiple in silico computational methods were used to identify non-synonymous or amino acid-changing SNPs (nsSNP) that are deleterious to TRIM22 structure and/or function. A sequence homology-based approach was adopted for screening nsSNPs in TRIM22, including six different in silico prediction algorithms and evolutionary conservation data from the ConSurf web server. In total, 14 high-risk nsSNPs were identified in TRIM22, most of which are located in a protein interaction module called the B30.2 domain. Additionally, 9 of the top high-risk nsSNPs altered the putative structure of TRIM22's B30.2 domain, particularly in the surface-exposed v2 and v3 regions. These same regions are critical for retroviral restriction by the closely-related TRIM5α protein. A number of putative structural and functional residues, including several sites that undergo post-translational modification, were also identified in TRIM22. This study is the first extensive in silico analysis of the highly polymorphic TRIM22 gene and will be a valuable resource for future targeted mechanistic and population-based studies.
format	article
author	Jenna N Kelly Stephen D Barr
author_facet	Jenna N Kelly Stephen D Barr
author_sort	Jenna N Kelly
title	In silico analysis of functional single nucleotide polymorphisms in the human TRIM22 gene.
title_short	In silico analysis of functional single nucleotide polymorphisms in the human TRIM22 gene.
title_full	In silico analysis of functional single nucleotide polymorphisms in the human TRIM22 gene.
title_fullStr	In silico analysis of functional single nucleotide polymorphisms in the human TRIM22 gene.
title_full_unstemmed	In silico analysis of functional single nucleotide polymorphisms in the human TRIM22 gene.
title_sort	in silico analysis of functional single nucleotide polymorphisms in the human trim22 gene.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/7bcda800c4f24e438fe945a80da6ee1d
work_keys_str_mv	AT jennankelly insilicoanalysisoffunctionalsinglenucleotidepolymorphismsinthehumantrim22gene AT stephendbarr insilicoanalysisoffunctionalsinglenucleotidepolymorphismsinthehumantrim22gene
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In silico analysis of functional single nucleotide polymorphisms in the human TRIM22 gene.

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