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Mass spectral data for 64 eluted peptides and structural modeling define peptide binding preferences for class I alleles in two chicken MHC-B haplotypes associated with opposite responses to Marek's disease

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Mass spectral data for 64 eluted peptides and structural modeling define peptide binding preferences for class I alleles in two chicken MHC-B haplotypes associated with opposite responses to Marek's disease

Content Provider	Springer Nature Link
Author	Sherman, Mark A. Goto, Ronald M. Moore, Roger E. Hunt, Henry D. Lee, Terry D. Miller, Marcia M.
Copyright Year	2008
Abstract	In the chicken, resistance to lymphomas that form following infection with oncogenic strains of Marek's herpesvirus is strongly linked to the major histocompatibility complex (MHC)-B complex. MHC-B21 haplotype is associated with lower tumor-related mortality compared to other haplotypes including MHC-B13. The single, dominantly expressed class I gene (BF2) is postulated as responsible for the MHC-B haplotype association. We used mass spectrometry to identify peptides and structural modeling to define the peptide binding preferences of BF22101 and BF21301 proteins. Endogenous peptides (8–12 residues long) were eluted from affinity-purified BF22101 and BF21301 proteins obtained from transduced cDNA expressed in RP9 cells, hence expressed in the presence of heterologous TAP. Sequences of individual peptides were identified by mass spectrometry. BF22101 peptides appear to be tethered at the binding groove margins with longer peptides arching out but selected by preferred residues at positions P3, P5, and P8: X-X-[AVILFP]-X(1–5)-[AVLFWP]-X(2–3)-[VILFM]. BF21301 peptides appear selected for residues at P2, P3, P5, and P8: X-[DE]-[AVILFW]-X(1–2)-[DE]-X-X-[ED]-X(0–4). Some longer BF21301 peptides likely also arch out, but others are apparently accommodated by repositioning of Arg83 so that peptides extend beyond the last preferred residue at P8. Comparisons of these peptides with earlier peptides derived in the presence of homologous TAP transport revealed the same side chain preferences. Scanning of Marek's and other viral proteins with the BF22101 motif identified many matches, as did the control human leukocyte antigen A0201 motif. The BF21301 motif is more restricting suggesting that this allele may confer a selective advantage only in infections with a subset of viral pathogens.
Starting Page	527
Ending Page	541
Page Count	15
File Format	PDF
ISSN	00937711
Journal	Immunogenetics
Volume Number	60
Issue Number	9
e-ISSN	14321211
Language	English
Publisher	Springer-Verlag
Publisher Date	2008-07-09
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Chicken MHC-B MHC class I Peptide binding motif BF22101 BF21301 Allergology Gene Function Cell Biology Human Genetics Immunology
Content Type	Text
Resource Type	Article
Subject	Genetics Immunology

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Mass spectral data for 64 eluted peptides and structural modeling define peptide binding preferences for class I alleles in two chicken MHC-B haplotypes associated with opposite responses to Marek's disease

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Mass spectral data for 64 eluted peptides and structural modeling define peptide binding preferences for class I alleles in two chicken MHC-B haplotypes associated with opposite responses to Marek's disease

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Mass spectral data for 64 eluted peptides and structural modeling define peptide binding preferences for class I alleles in two chicken MHC-B haplotypes associated with opposite responses to Marek's disease

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