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

Takeda E, Nakagawa S, Nakaya Y, Tanaka A, Miyazawa T, Yasuda J - PLoS ONE (2012)

Bottom Line: 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.On the other hand, bBST-2B may have a different physiological function from bBST-2A1 and bBST-2A2.

View Article: PubMed Central - PubMed

Affiliation: Department of Emerging Infectious Diseases, Institute of Tropical Medicine, Nagasaki University, Nagasaki, Japan.

ABSTRACT
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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Subcellular localization of bovine BST-2s.FLAG-tagged bBST-2s expressed in MDBK cells (left two lines) and HeLa cells (right two lines) were stained with FITC-conjugated anti-FLAG antibody (showed green) and then observed by fluorescence microscopy. Nuclei stained with DAPI are shown in blue the merged panels.
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pone-0041483-g004: Subcellular localization of bovine BST-2s.FLAG-tagged bBST-2s expressed in MDBK cells (left two lines) and HeLa cells (right two lines) were stained with FITC-conjugated anti-FLAG antibody (showed green) and then observed by fluorescence microscopy. Nuclei stained with DAPI are shown in blue the merged panels.

Mentions: We next examined the subcellular localization of bBST-2s by fluorescence microscopy. MDBK and HeLa cells expressing FLAG-tagged BST-2s were stained with FITC-conjugated anti-FLAG antibody (Figure 4). Both bBST-2A1 and bBST-2A2 showed a broad distribution in the cytoplasm of both MDBK and HeLa cells, while bBST-2B was mainly localized in the perinuclear compartment in both MDBK and HeLa cells.


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

Takeda E, Nakagawa S, Nakaya Y, Tanaka A, Miyazawa T, Yasuda J - PLoS ONE (2012)

Subcellular localization of bovine BST-2s.FLAG-tagged bBST-2s expressed in MDBK cells (left two lines) and HeLa cells (right two lines) were stained with FITC-conjugated anti-FLAG antibody (showed green) and then observed by fluorescence microscopy. Nuclei stained with DAPI are shown in blue the merged panels.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3401110&req=5

pone-0041483-g004: Subcellular localization of bovine BST-2s.FLAG-tagged bBST-2s expressed in MDBK cells (left two lines) and HeLa cells (right two lines) were stained with FITC-conjugated anti-FLAG antibody (showed green) and then observed by fluorescence microscopy. Nuclei stained with DAPI are shown in blue the merged panels.
Mentions: We next examined the subcellular localization of bBST-2s by fluorescence microscopy. MDBK and HeLa cells expressing FLAG-tagged BST-2s were stained with FITC-conjugated anti-FLAG antibody (Figure 4). Both bBST-2A1 and bBST-2A2 showed a broad distribution in the cytoplasm of both MDBK and HeLa cells, while bBST-2B was mainly localized in the perinuclear compartment in both MDBK and HeLa cells.

Bottom Line: 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.On the other hand, bBST-2B may have a different physiological function from bBST-2A1 and bBST-2A2.

View Article: PubMed Central - PubMed

Affiliation: Department of Emerging Infectious Diseases, Institute of Tropical Medicine, Nagasaki University, Nagasaki, Japan.

ABSTRACT
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.

Show MeSH
Related in: MedlinePlus