| タイトル |
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en
Single amino acid residue in the A2 domain of major histocompatibility complex class I is involved in the efficiency of equine herpesvirus-1 entry.
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| 作成者 |
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| アクセス権 |
open access |
| 主題 |
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| 内容注記 |
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Abstract
en
Equine herpesvirus-1 (EHV-1), an α-herpesvirus of the family Herpesviridae, causes respiratory disease, abortion, and encephalomyelitis in horses. EHV-1 utilizes equine MHC class I molecules as entry receptors. However, hamster MHC class I molecules on EHV-1-susceptible CHO-K1 cells play no role in EHV-1 entry. To identify the MHC class I molecule region that is responsible for EHV-1 entry, domain exchange and site-directed mutagenesis experiments were performed, in which parts of the extracellular region of hamster MHC class I (clone C5) were replaced with corresponding sequences from equine MHC class I (clone A68). Substitution of alanine for glutamine at position 173 (Q173A) within the α2 domain of the MHC class I molecule enabled hamster MHC class I C5 to mediate EHV-1 entry into cells. Conversely, substitution of glutamine for alanine at position 173 (A173Q) in equine MHC class I A68 resulted in loss of EHV-1 receptor function. Equine MHC class I clone 3.4, which possesses threonine at position 173, was unable to act as an EHV-1 receptor. Substitution of alanine for threonine at position 173 (T173A) enabled MHC class I 3.4 to mediate EHV-1 entry into cells. These results suggest that the amino acid residue at position 173 of the MHC class I molecule is involved in the efficiency of EHV-1 entry.
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| 出版者 |
en
American Society for Biochemistry and Molecular Biology
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| 日付 |
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| 言語 |
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| 資源タイプ |
journal article |
| 出版タイプ |
AM |
| 資源識別子 |
HDL
http://hdl.handle.net/2115/59850
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| 関連 |
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isVersionOf
DOI
https://doi.org/10.1074/jbc.M111.251751
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PMID
21949188
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| 収録誌情報 |
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PISSN
0021-9258
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EISSN
1083-351X
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NCID
AA00251083
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en
The Journal of biological chemistry
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巻286
号45
開始ページ39370
終了ページ39378
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| ファイル |
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| コンテンツ更新日時 |
2023-07-26 |
