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Phenotypic Divergence of P Proteins of Australian Bat Lyssavirus Lineages Circulating in Microbats and Flying Foxes
Bats are reservoirs of many pathogenic viruses, including the lyssaviruses rabies virus (RABV) and Australian bat lyssavirus (ABLV). Lyssavirus strains are closely associated with particular host reservoir species, with evidence of specific adaptation. Associated phenotypic changes remain poorly und...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8147779/ https://www.ncbi.nlm.nih.gov/pubmed/34064444 http://dx.doi.org/10.3390/v13050831 |
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author | Deffrasnes, Celine Luo, Meng-Xiao Wiltzer-Bach, Linda David, Cassandra T. Lieu, Kim G. Wang, Lin-Fa Jans, David A. Marsh, Glenn A. Moseley, Gregory W. |
author_facet | Deffrasnes, Celine Luo, Meng-Xiao Wiltzer-Bach, Linda David, Cassandra T. Lieu, Kim G. Wang, Lin-Fa Jans, David A. Marsh, Glenn A. Moseley, Gregory W. |
author_sort | Deffrasnes, Celine |
collection | PubMed |
description | Bats are reservoirs of many pathogenic viruses, including the lyssaviruses rabies virus (RABV) and Australian bat lyssavirus (ABLV). Lyssavirus strains are closely associated with particular host reservoir species, with evidence of specific adaptation. Associated phenotypic changes remain poorly understood but are likely to involve phosphoprotein (P protein), a key mediator of the intracellular virus–host interface. Here, we examine the phenotype of P protein of ABLV, which circulates as two defined lineages associated with frugivorous and insectivorous bats, providing the opportunity to compare proteins of viruses adapted to divergent bat species. We report that key functions of P protein in the antagonism of interferon/signal transducers and activators of transcription 1 (STAT1) signaling and the capacity of P protein to undergo nuclear trafficking differ between lineages. Molecular mapping indicates that these differences are functionally distinct and appear to involve modulatory effects on regulatory regions or structural impact rather than changes to defined interaction sequences. This results in partial but significant phenotypic divergence, consistent with “fine-tuning” to host biology, and with potentially distinct properties in the virus–host interface between bat families that represent key zoonotic reservoirs. |
format | Online Article Text |
id | pubmed-8147779 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-81477792021-05-26 Phenotypic Divergence of P Proteins of Australian Bat Lyssavirus Lineages Circulating in Microbats and Flying Foxes Deffrasnes, Celine Luo, Meng-Xiao Wiltzer-Bach, Linda David, Cassandra T. Lieu, Kim G. Wang, Lin-Fa Jans, David A. Marsh, Glenn A. Moseley, Gregory W. Viruses Brief Report Bats are reservoirs of many pathogenic viruses, including the lyssaviruses rabies virus (RABV) and Australian bat lyssavirus (ABLV). Lyssavirus strains are closely associated with particular host reservoir species, with evidence of specific adaptation. Associated phenotypic changes remain poorly understood but are likely to involve phosphoprotein (P protein), a key mediator of the intracellular virus–host interface. Here, we examine the phenotype of P protein of ABLV, which circulates as two defined lineages associated with frugivorous and insectivorous bats, providing the opportunity to compare proteins of viruses adapted to divergent bat species. We report that key functions of P protein in the antagonism of interferon/signal transducers and activators of transcription 1 (STAT1) signaling and the capacity of P protein to undergo nuclear trafficking differ between lineages. Molecular mapping indicates that these differences are functionally distinct and appear to involve modulatory effects on regulatory regions or structural impact rather than changes to defined interaction sequences. This results in partial but significant phenotypic divergence, consistent with “fine-tuning” to host biology, and with potentially distinct properties in the virus–host interface between bat families that represent key zoonotic reservoirs. MDPI 2021-05-04 /pmc/articles/PMC8147779/ /pubmed/34064444 http://dx.doi.org/10.3390/v13050831 Text en © 2021 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 | Brief Report Deffrasnes, Celine Luo, Meng-Xiao Wiltzer-Bach, Linda David, Cassandra T. Lieu, Kim G. Wang, Lin-Fa Jans, David A. Marsh, Glenn A. Moseley, Gregory W. Phenotypic Divergence of P Proteins of Australian Bat Lyssavirus Lineages Circulating in Microbats and Flying Foxes |
title | Phenotypic Divergence of P Proteins of Australian Bat Lyssavirus Lineages Circulating in Microbats and Flying Foxes |
title_full | Phenotypic Divergence of P Proteins of Australian Bat Lyssavirus Lineages Circulating in Microbats and Flying Foxes |
title_fullStr | Phenotypic Divergence of P Proteins of Australian Bat Lyssavirus Lineages Circulating in Microbats and Flying Foxes |
title_full_unstemmed | Phenotypic Divergence of P Proteins of Australian Bat Lyssavirus Lineages Circulating in Microbats and Flying Foxes |
title_short | Phenotypic Divergence of P Proteins of Australian Bat Lyssavirus Lineages Circulating in Microbats and Flying Foxes |
title_sort | phenotypic divergence of p proteins of australian bat lyssavirus lineages circulating in microbats and flying foxes |
topic | Brief Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8147779/ https://www.ncbi.nlm.nih.gov/pubmed/34064444 http://dx.doi.org/10.3390/v13050831 |
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