Identification and functional analysis of three isoforms of bovine BST-2.

Human BST-2 (hBST-2) has been identified as a cellular antiviral factor that blocks the release of various enveloped viruses. Orthologues of BST-2 have been identified in several species, including human, monkeys, pig, mouse, cat and sheep. All have been reported to possess antiviral activity. Dupli...

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Main Authors: Eri Takeda, So Nakagawa, Yuki Nakaya, Atsushi Tanaka, Takayuki Miyazawa, Jiro Yasuda
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2012-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3401110?pdf=render
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spelling doaj-4502db5b839349eebbf542d98775c6e92020-11-25T01:13:35ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0177e4148310.1371/journal.pone.0041483Identification and functional analysis of three isoforms of bovine BST-2.Eri TakedaSo NakagawaYuki NakayaAtsushi TanakaTakayuki MiyazawaJiro YasudaHuman BST-2 (hBST-2) has been identified as a cellular antiviral factor that blocks the release of various enveloped viruses. Orthologues of BST-2 have been identified in several species, including human, monkeys, pig, mouse, cat and sheep. All have been reported to possess antiviral activity. Duplication of the BST-2 gene has been observed in sheep and the paralogues are referred to as ovine BST-2A and BST2-B, although only a single gene corresponding to BST-2 has been identified in most species. In this study, we identified three isoforms of bovine BST-2, named bBST-2A1, bBST-2A2 and bBST-2B, in bovine cells treated with type I interferon, but not in untreated cells. Both bBST-2A1 and bBST-2A2 are posttranslationally modified by N-linked glycosylation and a GPI-anchor as well as hBST-2, while bBST-2B has neither of these modifications. Exogenous expression of bBST-2A1 or bBST-2A2 markedly reduced the production of bovine leukemia virus and vesicular stomatitis virus from cells, while the antiviral activity of bBST-2B was much weaker than those of bBST-2A1 and bBST-2A2. Our data suggest that bBST-2A1 and bBST-2A2 function as part of IFN-induced innate immunity against virus infection. On the other hand, bBST-2B may have a different physiological function from bBST-2A1 and bBST-2A2.http://europepmc.org/articles/PMC3401110?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Eri Takeda
So Nakagawa
Yuki Nakaya
Atsushi Tanaka
Takayuki Miyazawa
Jiro Yasuda
spellingShingle Eri Takeda
So Nakagawa
Yuki Nakaya
Atsushi Tanaka
Takayuki Miyazawa
Jiro Yasuda
Identification and functional analysis of three isoforms of bovine BST-2.
PLoS ONE
author_facet Eri Takeda
So Nakagawa
Yuki Nakaya
Atsushi Tanaka
Takayuki Miyazawa
Jiro Yasuda
author_sort Eri Takeda
title Identification and functional analysis of three isoforms of bovine BST-2.
title_short Identification and functional analysis of three isoforms of bovine BST-2.
title_full Identification and functional analysis of three isoforms of bovine BST-2.
title_fullStr Identification and functional analysis of three isoforms of bovine BST-2.
title_full_unstemmed Identification and functional analysis of three isoforms of bovine BST-2.
title_sort identification and functional analysis of three isoforms of bovine bst-2.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2012-01-01
description Human BST-2 (hBST-2) has been identified as a cellular antiviral factor that blocks the release of various enveloped viruses. Orthologues of BST-2 have been identified in several species, including human, monkeys, pig, mouse, cat and sheep. All have been reported to possess antiviral activity. Duplication of the BST-2 gene has been observed in sheep and the paralogues are referred to as ovine BST-2A and BST2-B, although only a single gene corresponding to BST-2 has been identified in most species. In this study, we identified three isoforms of bovine BST-2, named bBST-2A1, bBST-2A2 and bBST-2B, in bovine cells treated with type I interferon, but not in untreated cells. Both bBST-2A1 and bBST-2A2 are posttranslationally modified by N-linked glycosylation and a GPI-anchor as well as hBST-2, while bBST-2B has neither of these modifications. Exogenous expression of bBST-2A1 or bBST-2A2 markedly reduced the production of bovine leukemia virus and vesicular stomatitis virus from cells, while the antiviral activity of bBST-2B was much weaker than those of bBST-2A1 and bBST-2A2. Our data suggest that bBST-2A1 and bBST-2A2 function as part of IFN-induced innate immunity against virus infection. On the other hand, bBST-2B may have a different physiological function from bBST-2A1 and bBST-2A2.
url http://europepmc.org/articles/PMC3401110?pdf=render
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