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

Sasaki Michihito; Kim Eunmi; Igarashi Manabu; Ito Kimihito; Hasebe Rie; Fukushi Hideto; Sawa Hirofumi; Kimura Takashi

Title	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.
Creator	en Sasaki, Michihito NRID 1000070609403 en Kim, Eunmi en Igarashi, Manabu NRID 1000010374240 en Ito, Kimihito NRID 1000060396314 en Hasebe, Rie NRID 1000070431335 en Fukushi, Hideto NRID 1000010156763 en Sawa, Hirofumi NRID 1000030292006 en Kimura, Takashi NRID 1000090261338
Accessrights	open access
Subject	NDC 649
Description	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.
Publisher	en American Society for Biochemistry and Molecular Biology
Date	Issued2011-11-11
Language	eng
Resource Type	journal article
Version Type	AM
Identifier	HDL http://hdl.handle.net/2115/59850
Relation	isVersionOf DOI https://doi.org/10.1074/jbc.M111.251751 PMID 21949188
Journal	PISSN 0021-9258 EISSN 1083-351X NCID AA00251083 en The Journal of biological chemistry Volume Number286 Issue Number45 Page Start39370 Page End39378
File	fulltext Fig 1-8.pdf 5.44 MB (application/pdf) Issued2011-11-11 fulltext R1-F manuscript Bioedit.pdf 153.6 KB (application/pdf) Issued2011-11-11
Oaidate	2023-07-26