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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pubmed-34011102012-07-30 Identification and Functional Analysis of Three Isoforms of Bovine BST-2 Takeda, Eri Nakagawa, So Nakaya, Yuki Tanaka, Atsushi Miyazawa, Takayuki Yasuda, Jiro Research Article 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. Public Library of Science 2012-07-20 /pmc/articles/PMC3401110/ /pubmed/22911799 http://dx.doi.org/10.1371/journal.pone.0041483 Text en Takeda et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
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Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Takeda, Eri Nakagawa, So Nakaya, Yuki Tanaka, Atsushi Miyazawa, Takayuki Yasuda, Jiro |
spellingShingle |
Takeda, Eri Nakagawa, So Nakaya, Yuki Tanaka, Atsushi Miyazawa, Takayuki Yasuda, Jiro Identification and Functional Analysis of Three Isoforms of Bovine BST-2 |
author_facet |
Takeda, Eri Nakagawa, So Nakaya, Yuki Tanaka, Atsushi Miyazawa, Takayuki Yasuda, Jiro |
author_sort |
Takeda, Eri |
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 |
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. |
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Public Library of Science |
publishDate |
2012 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3401110/ |
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1611544217958481920 |