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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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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