An endogenous bornavirus‐like nucleoprotein in miniopterid bats retains the RNA‐binding properties of the original viral protein

Endogenous bornavirus‐like nucleoprotein elements (EBLNs) are sequences derived from bornaviral N genes in vertebrate genomes. Some EBLNs have been suggested to encode functional proteins in host cells; however, little is known about their evolution and functional relationship to the viral genes fro...

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Vydané v:FEBS letters Ročník 596; číslo 3; s. 323 - 337
Hlavní autori: Mukai, Yahiro, Horie, Masayuki, Kojima, Shohei, Kawasaki, Junna, Maeda, Ken, Tomonaga, Keizo
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: England 01.02.2022
Predmet:
Amino Acid Sequence
Animals
Bornaviridae - genetics
Bornaviridae - metabolism
Chiroptera - virology
co‐evolution
endogenous bornavirus‐like elements
evolution
exaptation
Humans
Miniopterus
Nucleoproteins - chemistry
Nucleoproteins - genetics
Nucleoproteins - metabolism
Protein Binding
RNA-binding proteins
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
RNA‐binding protein
vertebrates
Viral Proteins - genetics
Viral Proteins - metabolism
RNA-binding protein
exaptation
Miniopterus
endogenous bornavirus-like elements
co-evolution
ISSN:0014-5793, 1873-3468, 1873-3468
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Abstract Endogenous bornavirus‐like nucleoprotein elements (EBLNs) are sequences derived from bornaviral N genes in vertebrate genomes. Some EBLNs have been suggested to encode functional proteins in host cells; however, little is known about their evolution and functional relationship to the viral genes from which EBLNs originate. Here, we predicted functionality of EBLNs based on the properties of N as an RNA‐binding protein. We showed an EBLN in miniopterid bats (miEBLN‐1) has evolved under purifying selection and encodes an RNA‐binding protein (miEBLN‐1p) with biochemical properties similar to bornaviral N. Furthermore, we revealed miEBLN‐1p interacts with host RNA‐binding proteins, such as MOV10. These data suggest that miEBLN‐1p has been exapted as an RNA‐binding protein with similar properties to exogenous bornaviral N in miniopterid bats. This study shows that miniopterid bats have a gene derived from the N gene of an ancient bornavirus, named miEBLN‐1, which has evolved under purifying selection. Furthermore, miEBLN‐1 encodes an RNA‐binding protein that interacts with several cellular RNA‐binding proteins, such as MOV10, with biochemical properties similar to bornaviral N proteins. Altogether, we provide strong evidence for the exaptation of miEBLN‐1.
AbstractList Endogenous bornavirus-like nucleoprotein elements (EBLNs) are sequences derived from bornaviral N genes in vertebrate genomes. Some EBLNs have been suggested to encode functional proteins in host cells; however, little is known about their evolution and functional relationship to the viral genes from which EBLNs originate. Here, we predicted functionality of EBLNs based on the properties of N as an RNA-binding protein. We showed an EBLN in miniopterid bats (miEBLN-1) has evolved under purifying selection and encodes an RNA-binding protein (miEBLN-1p) with biochemical properties similar to bornaviral N. Furthermore, we revealed miEBLN-1p interacts with host RNA-binding proteins, such as MOV10. These data suggest that miEBLN-1p has been exapted as an RNA-binding protein with similar properties to exogenous bornaviral N in miniopterid bats.Endogenous bornavirus-like nucleoprotein elements (EBLNs) are sequences derived from bornaviral N genes in vertebrate genomes. Some EBLNs have been suggested to encode functional proteins in host cells; however, little is known about their evolution and functional relationship to the viral genes from which EBLNs originate. Here, we predicted functionality of EBLNs based on the properties of N as an RNA-binding protein. We showed an EBLN in miniopterid bats (miEBLN-1) has evolved under purifying selection and encodes an RNA-binding protein (miEBLN-1p) with biochemical properties similar to bornaviral N. Furthermore, we revealed miEBLN-1p interacts with host RNA-binding proteins, such as MOV10. These data suggest that miEBLN-1p has been exapted as an RNA-binding protein with similar properties to exogenous bornaviral N in miniopterid bats.
Endogenous bornavirus‐like nucleoprotein elements (EBLNs) are sequences derived from bornaviral N genes in vertebrate genomes. Some EBLNs have been suggested to encode functional proteins in host cells; however, little is known about their evolution and functional relationship to the viral genes from which EBLNs originate. Here, we predicted functionality of EBLNs based on the properties of N as an RNA‐binding protein. We showed an EBLN in miniopterid bats (miEBLN‐1) has evolved under purifying selection and encodes an RNA‐binding protein (miEBLN‐1p) with biochemical properties similar to bornaviral N. Furthermore, we revealed miEBLN‐1p interacts with host RNA‐binding proteins, such as MOV10. These data suggest that miEBLN‐1p has been exapted as an RNA‐binding protein with similar properties to exogenous bornaviral N in miniopterid bats. This study shows that miniopterid bats have a gene derived from the N gene of an ancient bornavirus, named miEBLN‐1, which has evolved under purifying selection. Furthermore, miEBLN‐1 encodes an RNA‐binding protein that interacts with several cellular RNA‐binding proteins, such as MOV10, with biochemical properties similar to bornaviral N proteins. Altogether, we provide strong evidence for the exaptation of miEBLN‐1.
Endogenous bornavirus‐like nucleoprotein elements (EBLNs) are sequences derived from bornaviral N genes in vertebrate genomes. Some EBLNs have been suggested to encode functional proteins in host cells; however, little is known about their evolution and functional relationship to the viral genes from which EBLNs originate. Here, we predicted functionality of EBLNs based on the properties of N as an RNA‐binding protein. We showed an EBLN in miniopterid bats (miEBLN‐1) has evolved under purifying selection and encodes an RNA‐binding protein (miEBLN‐1p) with biochemical properties similar to bornaviral N. Furthermore, we revealed miEBLN‐1p interacts with host RNA‐binding proteins, such as MOV10. These data suggest that miEBLN‐1p has been exapted as an RNA‐binding protein with similar properties to exogenous bornaviral N in miniopterid bats.
Author Kawasaki, Junna
Mukai, Yahiro
Tomonaga, Keizo
Horie, Masayuki
Kojima, Shohei
Maeda, Ken
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Keywords RNA-binding protein
exaptation
Miniopterus
endogenous bornavirus-like elements
co-evolution
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Snippet Endogenous bornavirus‐like nucleoprotein elements (EBLNs) are sequences derived from bornaviral N genes in vertebrate genomes. Some EBLNs have been suggested...
Endogenous bornavirus-like nucleoprotein elements (EBLNs) are sequences derived from bornaviral N genes in vertebrate genomes. Some EBLNs have been suggested...
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SubjectTerms Amino Acid Sequence
Animals
Bornaviridae - genetics
Bornaviridae - metabolism
Chiroptera - virology
co‐evolution
endogenous bornavirus‐like elements
evolution
exaptation
Humans
Miniopterus
Nucleoproteins - chemistry
Nucleoproteins - genetics
Nucleoproteins - metabolism
Protein Binding
RNA-binding proteins
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
RNA‐binding protein
vertebrates
Viral Proteins - genetics
Viral Proteins - metabolism
Title An endogenous bornavirus‐like nucleoprotein in miniopterid bats retains the RNA‐binding properties of the original viral protein
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https://www.ncbi.nlm.nih.gov/pubmed/35043395
https://www.proquest.com/docview/2621249869
https://www.proquest.com/docview/2718339764
Volume 596
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