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Evolution of TRIM5 and TRIM22 in Bats Reveals a Complex Duplication Process
The innate immunological response in mammals involves a diverse and complex network of many proteins. Over the last years, the tripartite motif-containing protein 5 (TRIM5) and 22 (TRIM22) have shown promise as restriction factors of a plethora of viruses that infect primates. Although there have be...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8879501/ https://www.ncbi.nlm.nih.gov/pubmed/35215944 http://dx.doi.org/10.3390/v14020345 |
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author | Fernandes, Alexandre P. Águeda-Pinto, Ana Pinheiro, Ana Rebelo, Hugo Esteves, Pedro J. |
author_facet | Fernandes, Alexandre P. Águeda-Pinto, Ana Pinheiro, Ana Rebelo, Hugo Esteves, Pedro J. |
author_sort | Fernandes, Alexandre P. |
collection | PubMed |
description | The innate immunological response in mammals involves a diverse and complex network of many proteins. Over the last years, the tripartite motif-containing protein 5 (TRIM5) and 22 (TRIM22) have shown promise as restriction factors of a plethora of viruses that infect primates. Although there have been studies describing the evolution of these proteins in a wide range of mammals, no prior studies of the TRIM6/34/5/22 gene cluster have been performed in the Chiroptera order. Here, we provide a detailed analysis of the evolution of this gene cluster in several bat genomes. Examination of different yangochiroptera and yinpterochiroptera bat species revealed a dynamic history of gene expansion occurring in TRIM5 and TRIM22 genes. Multiple copies of TRIM5 were found in the genomes of several bats, demonstrating a very low degree of conservation in the synteny of this gene among species of the Chiroptera order. Our findings also reveal that TRIM22 is often found duplicated in yangochiroptera bat species, an evolutionary phenomenon not yet observed in any other lineages of mammals. In total, we identified 31 TRIM5 and 19 TRIM22 amino acids to be evolving under positive selection, with most of the residues being placed in the PRYSPRY domain, known to be responsible for binding to the viral capsid during restriction in the primate orthologous TRIM proteins. Altogether, our results help to shed light on the distinctive role of bats in nature as reservoirs of viruses, many of which have become threatening zoonotic diseases through virus spillover in the last decades. |
format | Online Article Text |
id | pubmed-8879501 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88795012022-02-26 Evolution of TRIM5 and TRIM22 in Bats Reveals a Complex Duplication Process Fernandes, Alexandre P. Águeda-Pinto, Ana Pinheiro, Ana Rebelo, Hugo Esteves, Pedro J. Viruses Article The innate immunological response in mammals involves a diverse and complex network of many proteins. Over the last years, the tripartite motif-containing protein 5 (TRIM5) and 22 (TRIM22) have shown promise as restriction factors of a plethora of viruses that infect primates. Although there have been studies describing the evolution of these proteins in a wide range of mammals, no prior studies of the TRIM6/34/5/22 gene cluster have been performed in the Chiroptera order. Here, we provide a detailed analysis of the evolution of this gene cluster in several bat genomes. Examination of different yangochiroptera and yinpterochiroptera bat species revealed a dynamic history of gene expansion occurring in TRIM5 and TRIM22 genes. Multiple copies of TRIM5 were found in the genomes of several bats, demonstrating a very low degree of conservation in the synteny of this gene among species of the Chiroptera order. Our findings also reveal that TRIM22 is often found duplicated in yangochiroptera bat species, an evolutionary phenomenon not yet observed in any other lineages of mammals. In total, we identified 31 TRIM5 and 19 TRIM22 amino acids to be evolving under positive selection, with most of the residues being placed in the PRYSPRY domain, known to be responsible for binding to the viral capsid during restriction in the primate orthologous TRIM proteins. Altogether, our results help to shed light on the distinctive role of bats in nature as reservoirs of viruses, many of which have become threatening zoonotic diseases through virus spillover in the last decades. MDPI 2022-02-08 /pmc/articles/PMC8879501/ /pubmed/35215944 http://dx.doi.org/10.3390/v14020345 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Fernandes, Alexandre P. Águeda-Pinto, Ana Pinheiro, Ana Rebelo, Hugo Esteves, Pedro J. Evolution of TRIM5 and TRIM22 in Bats Reveals a Complex Duplication Process |
title | Evolution of TRIM5 and TRIM22 in Bats Reveals a Complex Duplication Process |
title_full | Evolution of TRIM5 and TRIM22 in Bats Reveals a Complex Duplication Process |
title_fullStr | Evolution of TRIM5 and TRIM22 in Bats Reveals a Complex Duplication Process |
title_full_unstemmed | Evolution of TRIM5 and TRIM22 in Bats Reveals a Complex Duplication Process |
title_short | Evolution of TRIM5 and TRIM22 in Bats Reveals a Complex Duplication Process |
title_sort | evolution of trim5 and trim22 in bats reveals a complex duplication process |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8879501/ https://www.ncbi.nlm.nih.gov/pubmed/35215944 http://dx.doi.org/10.3390/v14020345 |
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