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Single amino acid residue in the A2 domain of major histocompatibility complex class I is involved in the efficiency of equine herpesvirus-1 entry.
| Title: | Single amino acid residue in the A2 domain of major histocompatibility complex class I is involved in the efficiency of equine herpesvirus-1 entry. |
| Authors: | Sasaki, Michihito Browse this author →KAKEN DB | | Kim, Eunmi Browse this author | | Igarashi, Manabu Browse this author →KAKEN DB | | Ito, Kimihito Browse this author →KAKEN DB | | Hasebe, Rie Browse this author →KAKEN DB | | Fukushi, Hideto Browse this author →KAKEN DB | | Sawa, Hirofumi Browse this author →KAKEN DB | | Kimura, Takashi Browse this author →KAKEN DB |
| Issue Date: | 11-Nov-2011 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Journal Title: | The Journal of biological chemistry |
| Volume: | 286 |
| Issue: | 45 |
| Start Page: | 39370 |
| End Page: | 39378 |
| Publisher DOI: | 10.1074/jbc.M111.251751 |
| PMID: | 21949188 |
| Abstract: | 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. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/59850 |
| Appears in Collections: | 人獣共通感染症国際共同研究所 (International Institute for Zoonosis Control) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 佐々木 道仁
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