HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Research Center for Zoonosis Control >
Peer-reviewed Journal Articles, etc >

Single amino acid residue in the A2 domain of major histocompatibility complex class I is involved in the efficiency of equine herpesvirus-1 entry.

Files in This Item:
Fig 1-8.pdf5.57 MBPDFView/Open
R1-F manuscript Bioedit.pdf153.6 kBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/59850

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:人獣共通感染症リサーチセンター (Research Center for Zoonosis Control) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 佐々木 道仁

Export metadata:

OAI-PMH ( junii2 , jpcoar )


 

Feedback - Hokkaido University