Erratum to: Heterozygosity of the 721.221-B*51:01 Cell Line Used in the Study by Guasp et (Arthritis Rheumatol, 2016, 69, 3, 686, 10.1002/art.39430);The Peptidome of Behçet's Disease-Associated HLA-B∗51:01 Includes Two Subpeptidomes Differentially Shaped by Endoplasmic Reticulum Aminopeptidase 1

Arthritis and Rheumatology

Volumn 68, Issue 2, 2016, Pages 505-515

  Guasp, Pablo ^a   Alvarez Navarro, Carlos ^a   Gomez Molina, Patricia ^a   Martín Esteban, Adrian ^a   Marcilla, Miguel ^b   Barnea, Eilon ^c   Admon, Arie ^c   Lõpez De Castro, José A ^a  

^a CENTRO DE BIOLOGÍA MOLECULAR SEVERO OCHOA   (Spain)

^b CSIC   (Spain)

^c TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1; ENDOPLASMIC RETICULUM AMINOPEPTIDASE 2; HLA B ANTIGEN; PROTEIN; UNCLASSIFIED DRUG; ABC TRANSPORTER; AMINOPEPTIDASE; ERAP1 PROTEIN, HUMAN; ERAP2 PROTEIN, HUMAN; HLA B51 ANTIGEN; PEPTIDE; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING (TAP);

AFFINITY CHROMATOGRAPHY; ALGORITHM; ALLOTYPE; ANTIGEN PRESENTATION; ARTICLE; BEHCET DISEASE; BINDING AFFINITY; CONTROLLED STUDY; DISEASE ASSOCIATION; GENE SEQUENCE; HLA SYSTEM; HUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; TANDEM MASS SPECTROMETRY; WESTERN BLOTTING; CELL LINE; GENETICS; GENOTYPE; METABOLISM; SINGLE NUCLEOTIDE POLYMORPHISM;

AMINOPEPTIDASES; ATP-BINDING CASSETTE TRANSPORTERS; BEHCET SYNDROME; CELL LINE; CHROMATOGRAPHY, AFFINITY; GENOTYPE; HLA-B51 ANTIGEN; HUMANS; PEPTIDES; POLYMORPHISM, SINGLE NUCLEOTIDE; TANDEM MASS SPECTROMETRY;

EID: 84956745413     PISSN: 23265191     EISSN: 23265205     Source Type: Journal    
DOI: 10.1002/art.40073     Document Type: Erratum

References (50)

1. Momburg F, Roelse J, Howard JC, Butcher GW, Hammerling GJ, Neefjes JJ., Selectivity of MHC-encoded peptide transporters from human, mouse and rat. Nature 1994; 367: 648-51.
2. Saric T, Chang SC, Hattori A, York IA, Markant S, Rock KL, et al., An IFN-γ-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat Immunol 2002; 3: 1169-76.
3. Serwold T, Gonzalez F, Kim J, Jacob R, Shastri N., ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 2002; 419: 480-3.
4. Saveanu L, Carroll O, Lindo V, Del Val M, Lopez D, Lepelletier Y, et al., Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum. Nat Immunol 2005; 6: 689-97.
5. Elliott T, Williams A., The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex. Immunol Rev 2005; 207: 89-99.
6. Kuiper JJ, Van Setten J, Ripke S, Van 't Slot R, Mulder F, Missotten T, et al., A genome-wide association study identifies a functional ERAP2 haplotype associated with birdshot chorioretinopathy. Hum Mol Genet 2014; 23: 6081-7.
7. Brewerton DA, Hart FD, Nicholls A, Caffrey M, James DC, Sturrock RD., Ankylosing spondylitis and HL-A 27. Lancet 1973; 1: 904-7.
8. Tiilikainen A, Lassus A, Karvonen J, Vartiainen P, Julin M., Psoriasis and HLA-Cw6. Br J Dermatol 1980; 102: 179-84.
9. De Menthon M, LaValley MP, Maldini C, Guillevin L, Mahr A., HLA-B51/B5 and the risk of Behçet's disease: a systematic review and meta-analysis of case-control genetic association studies. Arthritis Rheum 2009; 61: 1287-96.
10. TASC and WTCCC2 Consortia. Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility. Nat Genet 2011; 43: 761-7.
11. Strange A, Capon F, Spencer CC, Knight J, Weale ME, Allen MH, et al., A genome-wide association study identifies new psoriasis susceptibility loci and an interaction between HLA-C and ERAP1. Nat Genet 2010; 42: 985-90.
12. Kirino Y, Bertsias G, Ishigatsubo Y, Mizuki N, Tugal-Tutkun I, Seyahi E, et al., Genome-wide association analysis identifies new susceptibility loci for Behçet's disease and epistasis between HLA-B∗51 and ERAP1. Nat Genet 2013; 45: 202-7.
13. Sakane T, Takeno M, Suzuki N, Inaba G., Behçet's disease. N Engl J Med 1999; 341: 1284-91.
14. Hill A, Takiguchi M, McMichael A., Different rates of HLA class I molecule assembly which are determined by amino acid sequence in the α2 domain. Immunogenetics 1993; 37: 95-101.
15. Kaslow RA, Carrington M, Apple R, Park L, Munoz A, Saah AJ, et al., Influence of combinations of human major histocompatibility complex genes on the course of HIV-1 infection. Nat Med 1996; 2: 405-11.
16. Falk K, Rotzschke O, Takiguchi M, Gnau V, Stevanovic S, Jung G, et al., Peptide motifs of HLA-B51, -B52 and -B78 molecules, and implications for Behçet's disease. Int Immunol 1995; 7: 223-8.
17. Sakaguchi T, Ibe M, Miwa K, Kaneko Y, Yokota S, Tanaka K, et al., Binding of 8-mer to 11-mer peptides carrying the anchor residues to slow assembling HLA class I molecules (HLA-B∗5101). Immunogenetics 1997; 45: 259-65.
18. Maenaka K, Maenaka T, Tomiyama H, Takiguchi M, Stuart DI, Jones EY., Nonstandard peptide binding revealed by crystal structures of HLA-B∗5101 complexed with HIV immunodominant epitopes. J Immunol 2000; 165: 3260-7.
19. Bassani-Sternberg M, Pletscher-Frankild S, Jensen LJ, Mann M., Mass spectrometry of human leukocyte antigen class I peptidomes reveals strong effects of protein abundance and turnover on antigen presentation. Mol Cell Proteomics 2015; 14: 658-73.
20. Vanhoof G, Goossens F, De Meester I, Hendriks D, Scharpe S., Proline motifs in peptides and their biological processing. FASEB J 1995; 9: 736-44.
21. Hearn A, York IA, Rock KL., The specificity of trimming of MHC class I-presented peptides in the endoplasmic reticulum. J Immunol 2009; 183: 5526-36.
22. Shimizu Y, DeMars R., Production of human cells expressing individual transferred HLA-A,-B,-C genes using an HLA-A,-B,-C null human cell line. J Immunol 1989; 142: 3320-8.
23. Zemmour J, Little AM, Schendel DJ, Parham P., The HLA-A,B "negative" mutant cell line C1R expresses a novel HLA-B35 allele, which also has a point mutation in the translation initiation codon. J Immunol 1992; 148: 1941-8.
24. Barnstable CJ, Bodmer WF, Brown G, Galfre G, Milstein C, Williams AF, et al., Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens: new tools for genetic analysis. Cell 1978; 14: 9-20.
25. Alvarez-Navarro C, Martin-Esteban A, Barnea E, Admon A, Lopez de Castro JA., ERAP1 polymorphism relevant to inflammatory disease shapes the peptidome of the birdshot chorioretinopathy-associated HLA-A∗29:02 antigen. Mol Cell Proteomics 2015; 14: 1770-80.
26. Garcia-Medel N, Sanz-Bravo A, Van Nguyen D, Galocha B, Gomez-Molina P, Martin-Esteban A, et al., Functional interaction of the ankylosing spondylitis-associated endoplasmic reticulum aminopeptidase 1 polymorphism and HLA-B27 in vivo. Mol Cell Proteomics 2012; 11: 1416-29.
27. Milner E, Gutter-Kapon L, Bassani-Strenberg M, Barnea E, Beer I, Admon A., The effect of proteasome inhibition on the generation of the human leukocyte antigen (HLA) peptidome. Mol Cell Proteomics 2013; 12: 1853-64.
28. Paradela A, Alvarez I, Garcia-Peydro M, Sesma L, Ramos M, Vazquez J, et al., Limited diversity of peptides related to an alloreactive T cell epitope in the HLA-B27-bound peptide repertoire results from restrictions at multiple steps along the processing-loading pathway. J Immunol 2000; 164: 329-37.
29. Cox J, Mann M., MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 2008; 26: 1367-72.
30. Cox J, Neuhauser N, Michalski A, Scheltema RA, Olsen JV, Mann M., Andromeda: a peptide search engine integrated into the MaxQuant environment. J Proteome Res 2011; 10: 1794-805.
31. Martin-Esteban A, Gomez-Molina P, Sanz-Bravo A, Lopez de Castro JA., Combined effects of ankylosing spondylitis-associated ERAP1 polymorphisms outside the catalytic and peptide-binding sites on the processing of natural HLA-B27 ligands. J Biol Chem 2014; 289: 3978-90.
32. Karosiene E, Lundegaard C, Lund O, Nielsen M., NetMHCcons: a consensus method for the major histocompatibility complex class I predictions. Immunogenetics 2012; 64: 177-86.
33. Diez-Rivero CM, Chenlo B, Zuluaga P, Reche PA., Quantitative modeling of peptide binding to TAP using support vector machine. Proteins 2010; 78: 63-72.
34. Fruci D, Ferracuti S, Limongi MZ, Cunsolo V, Giorda E, Fraioli R, et al., Expression of endoplasmic reticulum aminopeptidases in EBV-B cell lines from healthy donors and in leukemia/lymphoma, carcinoma, and melanoma cell lines. J Immunol 2006; 176: 4869-79.
35. Alvarez-Navarro C, Lopez de Castro JA., ERAP1 structure, function and pathogenetic role in ankylosing spondylitis and other MHC-associated diseases. Mol Immunol 2014; 57: 12-21.
36. Sanz-Bravo A, Campos J, Mazariegos MS, Lopez de Castro JA., Dominant role of the ERAP1 polymorphism R528K in shaping the HLA-B27 peptidome through differential processing determined by multiple peptide residues. Arthritis Rheumatol 2015; 67: 692-701.
37. Garcia-Medel N, Sanz-Bravo A, Alvarez-Navarro C, Gomez-Molina P, Barnea E, Marcilla M, et al., Peptide handling by HLA-B27 subtypes influences their biological behavior, association with ankylosing spondylitis and susceptibility to ERAP1. Mol Cell Proteomics 2014; 13: 3367-80.
38. Khan AR, Baker BM, Ghosh P, Biddison WE, Wiley DC., The structure and stability of an HLA-A∗0201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site. J Immunol 2000; 164: 6398-405.
39. Samino Y, Lopez D, Guil S, Saveanu L, van Endert PM, Del Val M., A long N-terminal-extended nested set of abundant and antigenic major histocompatibility complex class I natural ligands from HIV envelope protein. J Biol Chem 2006; 281: 6358-65.
40. Sakaguchi T, Ibe M, Miwa K, Yokota S, Tanaka K, Schonbach C, et al., Predominant role of N-terminal residue of nonamer peptides in their binding to HLA-B∗ 5101 molecules. Immunogenetics 1997; 46: 245-8.
41. Neisig A, Roelse J, Sijts AJ, Ossendorp F, Feltkamp MC, Kast WM, et al., Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences. J Immunol 1995; 154: 1273-9.
42. Hillen N, Mester G, Lemmel C, Weinzierl AO, Muller M, Wernet D, et al., Essential differences in ligand presentation and T cell epitope recognition among HLA molecules of the HLA-B44 supertype. Eur J Immunol 2008; 38: 2993-3003.
43. Reeves E, Edwards CJ, Elliott T, James E., Naturally occurring ERAP1 haplotypes encode functionally distinct alleles with fine substrate specificity. J Immunol 2013; 191: 35-43.
44. Kaneko F, Takahashi Y, Muramatsu R, Adachi K, Miura Y, Nakane A, et al., Natural killer cell numbers and function in peripheral lymphoid cells in Behçet's disease. Br J Dermatol 1985; 113: 313-8.
45. Hamzaoui K, Ayed K, Hamza M, Touraine JL., Natural killer cells in Behçet's disease. Clin Exp Immunol 1988; 71: 126-31.
46. Suzuki Y, Hoshi K, Matsuda T, Mizushima Y., Increased peripheral blood γδ+ T cells and natural killer cells in Behçet's disease. J Rheumatol 1992; 19: 588-92.
47. Cifaldi L, Romania P, Falco M, Lorenzi S, Meazza R, Petrini S, et al., ERAP1 regulates natural killer cell function by controlling the engagement of inhibitory receptors. Cancer Res 2015; 75: 824-34.
48. Motozono C, Kuse N, Sun X, Rizkallah PJ, Fuller A, Oka S, et al., Molecular basis of a dominant T cell response to an HIV reverse transcriptase 8-mer epitope presented by the protective allele HLA-B∗51:01. J Immunol 2014; 192: 3428-34.
49. Yager N, Robinson N, Brown H, Flanagan P, Frater J, Fidler S, et al., SPARTAC Trial Investigators. Longitudinal analysis of an HLA-B∗51-restricted epitope in integrase reveals immune escape in early HIV-1 infection. AIDS 2013; 27: 313-23.
50. Conde-Jaldon M, Montes-Cano MA, Garcia-Lozano JR, Ortiz-Fernandez L, Ortego-Centeno N, Gonzalez-Leon R, et al., Epistatic interaction of ERAP1 and HLA-B in Behçet disease: a replication study in the Spanish population. PLoS One 2014; 9: e102100.