Identification of amino acids in the human tetherin transmembrane domain responsible for HIV-1 Vpu interaction and susceptibility.
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抄録
Tetherin, also known as BST-2/CD317/HM1.24, is an antiviral cellular protein that inhibits the release of HIV-1 particles from infected cells. HIV-1 viral protein U (Vpu) is a specific antagonist of human tetherin that might contribute to the high virulence of HIV-1. In this study, we show that three amino acid residues (I34, L37, and L41) in the transmembrane (TM) domain of human tetherin are critical for the interaction with Vpu by using a live cell-based assay. We also found that the conservation of an additional amino acid at position 45 and two residues downstream of position 22, which are absent from monkey tetherins, are required for the antagonism by Vpu. Moreover, computer-assisted structural modeling and mutagenesis studies suggest that an alignment of these four amino acid residues (I34, L37, L41, and T45) on the same helical face in the TM domain is crucial for the Vpu-mediated antagonism of human tetherin. These results contribute to the molecular understanding of human tetherin-specific antagonism by HIV-1 Vpu.
収録刊行物
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- Journal of virology
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Journal of virology 85 (2), 932-945, 2011-01
American Society for Microbiology
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キーワード
- Amino Acids/genetics
- Amino Acids/metabolism
- Animals
- Antigens, CD/genetics
- Antigens, CD/metabolism
- Cell Line
- GPI-Linked Proteins/genetics
- GPI-Linked Proteins/metabolism
- HIV-1/pathogenicity
- Human Immunodeficiency Virus Proteins/metabolism
- Humans
- Models, Molecular
- Protein Binding
- Protein Interaction Mapping
- Protein Structure, Tertiary
- Viral Regulatory and Accessory Proteins/metabolism
詳細情報 詳細情報について
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- CRID
- 1050001201940530560
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- NII論文ID
- 120002723154
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- NII書誌ID
- AA00708779
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- ISSN
- 0022538X
- 10985514
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- HANDLE
- 2433/134599
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- IRDB
- Crossref
- CiNii Articles
- KAKEN
