Analysis of MHC class I genes across horse MHC haplotypes

Tallmadge, Rebecca L.; Campbell, Julie A.; Miller, Donald C.; Antczak, Douglas F.

doi:10.1007/s00251-009-0420-9

Cited by 49 publications

(67 citation statements)

References 57 publications

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“…Equine MHC class I allele (Eqca)-N*00602 (formerly designated as the equine MHC I 7-6 allele) is associated with the serologically defined ELA-A1 alleles (19,(23)(24)(25), which are prevalent in the Arabian horse and mixed-breed pony. Another ELA allele, Eqca-N*00601, formerly designated as the equine MHC I 114 allele, which differs from Eqca-N*00602 allele by a single amino acid (E152V) within the peptide-binding groove (20,25), resulted in the abrogation of epitope peptide Gag-GW12-specific CTL recognition even though Gag-GW12 can still bind to Eqca-N*00601 (20). This phenomenon highlights the immunologic importance of MHC I polymorphism for antiviral immunity.…”

mentioning

confidence: 99%

Structural Illumination of Equine MHC Class I Molecules Highlights Unconventional Epitope Presentation Manner That Is Evolved in Equine Leukocyte Antigen Alleles

Yao

et al. 2016

The Journal of Immunology

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MHC class I (MHC I)–restricted virus-specific CTLs are implicated as critical components in the control of this naturally occurring lentivirus and in the protective immune response to the successfully applied attenuated equine infectious anemia virus vaccine in the horse. Nevertheless, the structural basis for how the equine MHC I presents epitope peptides remains unknown. In this study, we investigated the binding of several equine infectious anemia virus–derived epitope peptides by the ability to refold recombinant molecules and by thermal stability, and then by determining the x-ray structure of five peptide–MHC I complexes: equine MHC class I allele (Eqca)-N*00602/Env-RW12, Eqca-N*00602/Gag-GW12, Eqca-N*00602/Rev-QW11, Eqca-N*00602/Gag-CF9, and Eqca-N*00601/Gag-GW12. Although Eqca-N*00601 and Eqca-N*00602 differ by a single amino acid, Eqca-N*00601 exhibited a drastically different peptide presentation when binding a similar CTL epitope, Gag-GW12; the result makes the previously reported function clear to be non–cross-recognition between these two alleles. The structures plus Eqca-N*00602 complexed with a 9-mer peptide are particularly noteworthy in that we illuminated differences in apparent flexibility in the center of the epitope peptides for the complexes with Gag-GW12 as compared with Env-RW12, and a strict selection of epitope peptides with normal length. The featured preferences and unconventional presentations of long peptides by equine MHC I molecules provide structural bases to explain the exceptional anti-lentivirus immunity in the horse. We think that the beneficial reference points could serve as an initial platform for other human or animal lentiviruses.

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confidence: 99%

Structural Illumination of Equine MHC Class I Molecules Highlights Unconventional Epitope Presentation Manner That Is Evolved in Equine Leukocyte Antigen Alleles

Yao

et al. 2016

The Journal of Immunology

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“…Equine MHC Class I with Threonine at Position 173 Is Unable to Act as an EHV-1 Receptor-Some equine MHC class I genes reportedly have valine, glutamic acid, or threonine instead of alanine at the position corresponding to position 173 of A68 (16). Among the equine MHC class I nucleotide sequences registered in GenBank, we successfully obtained the equine MHC class I clone 3.4 cDNA, which has a threonine residue at position 173, from primary equine cells by RT-PCR (Fig.…”

Section: Hydrophobicity Of the Amino Acid At Residue 173 In Equine Mhmentioning

confidence: 99%

“…MHC class I is polygenic and polymorphic (15). Fifty equine MHC class I genes were identified among 10 different serologically defined equine MHC class I haplotypes (16), and seven MHC class I loci were transcribed in an MHC homozygous individual (17). Although previous studies have shown that three equine MHC class I molecules can act as EHV-1 receptors (13,14), it is unclear whether all MHC class I molecules are involved in EHV-1 infection.…”

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confidence: 99%

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

Kim

Igarashi

et al. 2011

Journal of Biological Chemistry

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Equine herpesvirus-1 (EHV-1), 2 an ␣-herpesvirus of the family Herpesviridae, is the causative agent of respiratory disease, abortion, and a serious neurological disease known as encephalomyelitis in horses. Currently available vaccines are insufficient to protect against neurological disorders and abortions caused by EHV-1 (1). Outbreaks of EHV-1 encephalomyelitis can devastate farms, riding schools, and veterinary hospitals (2-4). Therefore, EHV-1 is one of the most important pathogens in the equine industry.EHV-1 attaches to heparan sulfate on the cell surface (5, 6). Viral entry into cells occurs through either direct fusion at the plasma membrane or endocytosis (7,8). Among the viral glycoproteins that play important roles in EHV-1 entry, glycoprotein D (gD) is essential for viral entry in all cases (9 -12). Recently, the equine MHC class I molecule was identified as a host factor involved in the entry process of EHV-1 (13, 14). NIH3T3 mouse fibroblast cells and B78H1 mouse melanoma cells are naturally resistant to EHV-1 infection; however, these cell lines become susceptible to EHV-1 infection by the exogenous expression of equine MHC class I (13, 14). The equine MHC class I molecule interacts with EHV-1 gD and mediates EHV-1 entry into equine cell types that are naturally susceptible to EHV-1 infection (14).MHC class I molecules are known primarily for their role in presenting peptides from intracellular antigens to cytotoxic T cells. MHC class I is polygenic and polymorphic (15). Fifty equine MHC class I genes were identified among 10 different serologically defined equine MHC class I haplotypes (16), and seven MHC class I loci were transcribed in an MHC homozygous individual (17). Although previous studies have shown that three equine MHC class I molecules can act as EHV-1 receptors (13,14), it is unclear whether all MHC class I molecules are involved in EHV-1 infection.Chinese hamster ovary (CHO)-K1 cells are known to be susceptible to EHV-1 infection (10). Unlike equine cells, inhibition of the cell surface expression of MHC class I molecules by ␤2-microglobulin knockdown does not reduce the susceptibility of CHO-K1 cells to EHV-1 infection (14). This result suggests that hamster MHC class I has no role in EHV-1 entry into CHO-K1 cells.In this study, we expressed hamster MHC class I on NIH3T3 cells and confirmed the inability of hamster MHC class I to mediate the cellular entry of EHV-1. To clarify the region of equine MHC class I responsible for EHV-1 entry, we performed domain exchange and site-directed mutagenesis experiments on the hamster MHC class I backbone, in which parts of the extracellular region were replaced with corresponding sequences from equine MHC class I. Results from these experiments revealed an important amino acid residue of MHC class *

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“…Antczak, personal communication). The genes from which the alleles originated had previously been assigned to four MHC class I loci (Supplementary File 3; see (Tallmadge et al, 2010) for nomenclature). To capture any additional alleles, generic RT-PCR primers were also used (adapted from (Chung et al, 2003)) that closely matched homologous regions of all the classical MHC class I genes but did not bind to known non-classical and pseudogene sequences.…”

Section: Rt-pcrs For Mhc Class I Genotypingmentioning

confidence: 99%

“…Equine MHC class I genes and primers used to amplify specific alleles by RT-PCR. Tallmadge et al (2010).^primers adapted from Chung et al (2003) N/A = not applicable…”

Section: 1(b2)mentioning

confidence: 99%

Polarisation of equine pregnancy outcome associated with a maternal MHC class I allele: Preliminary evidence

Kydd

Case

Winton

et al. 2016

Veterinary Microbiology

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Kydd, Julia H. (2016) Polarisation of equine pregnancy outcome associated with a maternal MHC class I allele: preliminary evidence. Veterinary Microbiology, 188 . pp. 34-40. ISSN 1873-2542 Access from the University of Nottingham repository: http://eprints.nottingham.ac.uk/32717/1/Kydd%20et%20al%202016%20eprint.pdf Copyright and reuse:The Nottingham ePrints service makes this work by researchers of the University of Nottingham available open access under the following conditions. This article is made available under the Creative Commons Attribution Non-commercial No Derivatives licence and may be reused according to the conditions of the licence. For more details see: http://creativecommons.org/licenses/by-nc-nd/2.5/ A note on versions:The version presented here may differ from the published version or from the version of record. If you wish to cite this item you are advised to consult the publisher's version. Please see the repository url above for details on accessing the published version and note that access may require a subscription.

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Analysis of MHC class I genes across horse MHC haplotypes

Cited by 49 publications

References 57 publications

Structural Illumination of Equine MHC Class I Molecules Highlights Unconventional Epitope Presentation Manner That Is Evolved in Equine Leukocyte Antigen Alleles

Structural Illumination of Equine MHC Class I Molecules Highlights Unconventional Epitope Presentation Manner That Is Evolved in Equine Leukocyte Antigen Alleles

Single Amino Acid Residue in the A2 Domain of Major Histocompatibility Complex Class I Is Involved in the Efficiency of Equine Herpesvirus-1 Entry

Polarisation of equine pregnancy outcome associated with a maternal MHC class I allele: Preliminary evidence

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