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The peptide specificity of HLA-B*1403, an allotype associated with ankylosing spondylitis (Lopez-Larrea, C., Mijiyawa, M., Gonzalez, S., Fernandez-Morera, J. L., Blanco-Gelaz, M. A., Martinez-Borra, J., and Lopez-Vazquez, A. (2002) Arthritis Rheum. 46, 2968–2971) was compared with those of the non-associated B*1402 and the prototypic disease-associated B*2705 allotypes. Although differing by a single residue (L156R), B*1402 and B*1403 shared only 32–35% of their peptide repertoires. Subtype-related differences observed in multiple peptide positions, including P3 and P7, were largely explained by a direct effect of the L156R change on peptide specificity. The HLA-B14 subtypes shared only ∼3% of their peptide repertoires with B*2705. This was due to distinct residue usage at most positions, as revealed by statistical comparison of B*1402, B*1403, and B*2705-bound nonamers. Nevertheless, shared ligands between B*2705 and B*1403 were formally identified, although ligands common to B*2705 and B*1403, but absent from B*1402, were not found. Alloreactive T-cells were used as a tool to analyze epitope sharing among B*1402, B*1403, and B*2705. The percentage of cross-reactive T-cell clones closely paralleled peptide overlap, suggesting that shared ligands tend to maintain their antigenic features when bound to the different allotypes. Our results indicate that B*1403 and B*2705 can present common peptides. However, both the disparity of their peptide repertoires and the lack of binding features shared by these two allotypes, but not B*1402, argue against, although do not exclude, a mechanism of spondyloarthritis mediated by specific ligands of B*2705 and B*1403. The peptide specificity of HLA-B*1403, an allotype associated with ankylosing spondylitis (Lopez-Larrea, C., Mijiyawa, M., Gonzalez, S., Fernandez-Morera, J. L., Blanco-Gelaz, M. A., Martinez-Borra, J., and Lopez-Vazquez, A. (2002) Arthritis Rheum. 46, 2968–2971) was compared with those of the non-associated B*1402 and the prototypic disease-associated B*2705 allotypes. Although differing by a single residue (L156R), B*1402 and B*1403 shared only 32–35% of their peptide repertoires. Subtype-related differences observed in multiple peptide positions, including P3 and P7, were largely explained by a direct effect of the L156R change on peptide specificity. The HLA-B14 subtypes shared only ∼3% of their peptide repertoires with B*2705. This was due to distinct residue usage at most positions, as revealed by statistical comparison of B*1402, B*1403, and B*2705-bound nonamers. Nevertheless, shared ligands between B*2705 and B*1403 were formally identified, although ligands common to B*2705 and B*1403, but absent from B*1402, were not found. Alloreactive T-cells were used as a tool to analyze epitope sharing among B*1402, B*1403, and B*2705. The percentage of cross-reactive T-cell clones closely paralleled peptide overlap, suggesting that shared ligands tend to maintain their antigenic features when bound to the different allotypes. Our results indicate that B*1403 and B*2705 can present common peptides. However, both the disparity of their peptide repertoires and the lack of binding features shared by these two allotypes, but not B*1402, argue against, although do not exclude, a mechanism of spondyloarthritis mediated by specific ligands of B*2705 and B*1403. The association of HLA-B27 with spondyloarthropathies and, in particular, ankylosing spondylitis (AS) 2The abbreviations used are:ASankylosing spondylitisCTLcytotoxic T lymphocyteC1RHmy2.C1RLCLlymphoblastoid cell linemAbmonoclonal antibodyHPLChigh performance liquid chromatographyMSmass spectrometryMALDI-TOFmatrix-assisted laser desorption ionization time-of-flightPBMCperipheral blood mononuclear cellm/zmass-to-charge ratioTAPtransporter associated with antigen processing is, by far, the strongest one between an HLA class I molecule and any disease (1Brewerton D.A. Hart F.D. Nicholls A. Caffrey M. James D.C. Sturrock R.D. Lancet. 1973; 1: 904-907Abstract PubMed Scopus (1458) Google Scholar, 2Schlosstein L. Terasaki P.I. Bluestone R. Pearson C.M. N. Engl. J. Med. 1973; 288: 704-706Crossref PubMed Scopus (1062) Google Scholar). The property of HLA-B27 that determines disease susceptibility remains unknown, and several pathogenetic mechanisms are currently being considered as a basis for various research lines (3Ramos M. Lopez de Castro J.A. Tissue Antigens. 2002; 60: 191-205Crossref PubMed Scopus (99) Google Scholar, 4Colbert R.A. Curr. Mol. Med. 2004; 4: 21-30Crossref PubMed Scopus (66) Google Scholar). One of these mechanisms is proposed by the arthritogenic peptide hypothesis (5Benjamin R. Parham P. Immunol. Today. 1990; 11: 137-142Abstract Full Text PDF PubMed Scopus (350) Google Scholar), which assumes that an initial pathogenetic event would be a cytotoxic T lymphocyte (CTL) response against an external antigen, whose molecular mimicry with a constitutive peptide ligand of HLA-B27 would elicit an autoimmune reaction against this molecule, leading to tissue damage and inflammation. This hypothesis, which emphasizes the antigen-presenting specificity of HLA-B27 as a critical pathogenetic feature, has stimulated studies on the nature of HLA-B27-bound peptide repertoires and their relationship to those presented by other class I molecules. A major feature of HLA-B27 ligands is the presence of R2 (6Jardetzky T.S. Lane W.S. Robinson R.A. Madden D.R. Wiley D.C. Nature. 1991; 353: 326-329Crossref PubMed Scopus (735) Google Scholar, 7Lopez de Castro J.A. Alvarez I. Marcilla M. Paradela A. Ramos M. Sesma L. Vazquez M. Tissue Antigens. 2004; 63: 424-445Crossref PubMed Scopus (85) Google Scholar), which binds tightly into the B pocket of the D.R. Wiley D.C. Nature. 1991; 353: PubMed Scopus Google Scholar, D.R. Wiley D.C. Full Text PDF PubMed Scopus Google Scholar). this pocket is of that are among HLA class I other HLA-B27 with this was of that an allotype that with this M. PubMed Scopus Google and binds in HLA-B27 ligands N. M. Arthritis Rheum. PubMed Scopus Google Scholar), was among in a in A. N. M. A. Arthritis Rheum. PubMed Scopus Google Scholar). was associated with the of Google Scholar), a of this disease that is to HLA-B27 Med. 2002; PubMed Scopus Google Scholar). of spondyloarthropathies in has with these class I that with R2 J.A. A. J. Immunol. PubMed Scopus Google Scholar). ankylosing spondylitis cytotoxic T lymphocyte cell performance liquid laser desorption ionization blood mononuclear cell associated with antigen processing B*1403, an allotype only in the of and I. Tissue Antigens. PubMed Scopus Google Scholar, M. J. A. Arthritis Rheum. 2002; PubMed Scopus Google Scholar), was associated to in the both this disease and HLA-B27 are M. J. A. Arthritis Rheum. 2002; PubMed Scopus Google Scholar). that be and were of the B*1403 The of this allotype in the was The closely allotype B*1402, which from B*1403 only at residue in in was in of the but was absent among B*1402 has a including among and has associated with of M. J. J. Full Text PDF PubMed Google revealed a of this allotype for with the B of B*1402 and B*1403 are was that this allotype would with this The of two closely HLA-B14 associated with for the to for peptide differences that with disease susceptibility in a was to for in peptide between HLA-B27 and but class I molecule, B*1403 from B*2705 in in the of the molecule, of which are in the and in this the peptide binding specificity of B*1402 and B*1403, to the between their constitutive peptide repertoires and the features of shared and bound that peptide sharing between B*1403 and B*2705 is although both common and the molecular basis of their peptide specificity. which a of the bound to the molecule A. 1991; PubMed Scopus Google Scholar, J. Med. 1991; PubMed Scopus Google Scholar, J. Immunol. Google Scholar), were used to analyze the relationship between epitope and peptide sharing among B*1402, B*1403, and B*2705. and is a cell with of HLA class I R.D. P. J. Immunol. Google Scholar, J. Parham P. J. Immunol. Google Scholar). with of HLA-B27 were Lopez Lopez de Castro J.A. J. Immunol. 1990; Google Scholar). B*1402 and B*1403 were as was from the cell B*1402, of B*1402 was by two in the and The was into the to that to the B*1402 into and into by at and as Lopez Lopez de Castro J.A. J. Immunol. 1990; Google Scholar). One single at B*1403 from B*1402 to The B*1403 was by of the B*1402 from were the an in the and an the were The reaction used an in the and a with the A reaction was both and from The was into and to that to the B*1403 the was into and into as cell lines were in with from used in this were specific for a HLA class I A. Full Text PDF PubMed Scopus Google and specific for Parham P. J. Immunol. PubMed Scopus Google Scholar). were in of and in of for were in of in of for and in of were at was in an the of and B*2705-bound and were from of the as A. M. Vazquez J. Lopez de Castro J.A. J. Immunol. Google Scholar). were in in the presence of a of cell were to the and peptide were with at and to performance liquid This was in a a at a of as A. Alvarez I. M. Sesma L. Ramos M. Vazquez J. Lopez de Castro J.A. J. Immunol. PubMed Scopus Google Scholar). of were and peptide of was by laser desorption ionization a with the in were in of and This was the and to at of in and at was and the was to at was by in an as J. Vazquez J. Lopez de Castro J.A. Tissue Antigens. PubMed Scopus Google Scholar, A. J. Lopez de Castro J.A. Vazquez J. J. PubMed Scopus Google Scholar). were an of as were in A in and a with and in a the with a of B in at were by between and were the which specific peptide to be The of was but by various including and a of the P. PubMed Scopus Google Scholar). the was used to for of peptide with the and clones against B*1402 were from various with the as blood mononuclear were stimulated in with a of and at and a were by of stimulated T in and in the presence of of in the statistical of were for HLA-B14 a against and as a lymphocyte were in with I with and from and T-cell clones were in the and in the presence of as Alloreactive clones against B*2705 were by the with the from various were stimulated in with the for a with the in lymphocyte for and with the initial by clones were used R. Lopez de Castro J.A. J. Immunol. Google Scholar). was by the with the on the of the being of were considered as between the of B*1402 and peptide from both subtypes were with and from the whose of B*1402 and B*1403 was peptide were by in and of the was by The of from one was compared with the and from the other to into in the of that in with the in this were considered to ligands of both in only one peptide were considered to This has used to the between HLA-B27 peptide repertoires in several studies from L. A. Vazquez J. Lopez de Castro J.A. J. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar, M. Paradela A. Vazquez M. A. Vazquez J. Lopez de Castro J.A. J. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar). were and the between the B*1402 and B*1403 peptide repertoires was as the of the two the basis of this B*1402 and B*1403 shared only of their peptide repertoires. The peptide in both was and a of class with an molecular of and for B*1402 and B*1403, both the molecular and of ligands were between both results indicate their B*1402 and B*1403 largely distinct peptide although this has effect on peptide of peptide ligands from B*1402 and of of shared of in a of and B*2705-bound peptides. of the peptide from the allotypes. of the bound to B*1402 B*1403. of the bound to B*1403 B*2705. are of two between HLA-B14 and and peptide repertoires were compared with that of the as for the two HLA-B14 B*1402 and B*1403 from B*2705 in and of their peptide This is a a comparison on and molecular in peptide the different are the peptide of peptide the and molecular that were from both B*1403 and B*2705 and to and different these results are to the peptide the of the B*2705-bound peptide with that of B*1403 would be and the of the with that of B*2705 would be of peptide ligands from B*1402, B*1403 and of of shared of of of shared of in a The molecular of the B*2705-bound was those of B*1402 B*1403 ligands and suggesting differences in peptide both between the and peptide repertoires This was from the of the between B*2705 and B*1402 B*1403 in the and the was for shared between B*2705 and B*1402 B*1403 an molecular and the B*1402 B*1403 ligands and the B*2705 ligands The of from B*1402 and B*1403 were those from B*2705 in are several for this be a of the of to HLA-B14 subtypes However, this was not by the that the peptide of the and were not a of the not in the used for peptide This is is a for in the of the class I whose is the are at a of B*2705 ligands by due to Although is for not this and formally is that the peptide is that of B*2705. This from residue usage at a of peptide among B*1402 and B*1403 ligands these results indicate that B*2705 with B*1402 and B*1403 only a of constitutive peptide and that binds with molecular Our results are with the that the B*2705-bound peptide is those of B*1402 and B*1403. B*1402 and B*1403 at of HLA-B14 ligands were by shared ligands of both and the peptide of both subtypes the of residue at among the from were the only to of with the the peptide of B*1402 were from including the shared and the nonamers. the peptide of B*1403 were from including the shared and the nonamers. A peptide was considered to when a residue of at that in at of the from a this basis B*1402 and B*1403 residue usage at and of the peptide positions, subtypes with the and which was to the other multiple residue subtypes in common a lack of in residue usage at to the of whose features are both subtypes differences in residue usage at and B*1402 at and and at P3 and B*1403 an at a of at although this was and were at this an at and a one at However, due to the of shared ligands in the the differences in residue were not at P3 and The peptide of B*1402 were in a M. J. J. Full Text PDF PubMed Google Scholar). that an of at P3 and was found. Our results are in with these for the at which were not by of B*1402 and B*1403 at among the from are both for and for residue and and and and and and residue a are and as peptide but a between subtypes and in are differences in residue among the from both subtypes were with the not of of residue was for only the of shared those that a of and were in both subtypes a among shared nonamers. those that different residue usage among a was observed in the of shared in B*1402, was and P3 an in B*1403, an at P7, both subtypes distinct the of shared ligands shared ligands at of peptide positions, the most being at HLA-B14 at basis for the disparity between the and peptide repertoires was by the features of A comparison of residue between the revealed a of differences was to among but not among the was to and among and was in the However, the differences in these two not statistical A was observed at were and were the among and differences were were among nonamers. was observed at were in the a was observed in B*1403, both statistical The of at in B*1402, to B*1403, was not a to was observed in both only were in the was differences were not the L156R change between B*1402 and B*1403 peptide specificity by residue in at peptide and The differences in residue observed at other and residue from the of peptide for between B*1403, and B*2705 of and in B*1403 but not in B*2705 were in this comparison these were as shared as ligands in the comparison B*2705 ligands and not in B*1403 were were HLA-B27 ligands de Castro J.A. Alvarez I. Marcilla M. Paradela A. Ramos M. Sesma L. Vazquez M. Tissue Antigens. 2004; 63: 424-445Crossref PubMed Scopus (85) Google and are for the The basis for the disparity between the and B*2705-bound peptide repertoires was by of a statistical comparison of residue usage between the and a de Castro J.A. Alvarez I. Marcilla M. Paradela A. Ramos M. Sesma L. Vazquez M. Tissue Antigens. 2004; 63: 424-445Crossref PubMed Scopus (85) Google of B*2705-bound The of B*1403 including both shared ligands with and were differences in residue usage between B*1403 and B*2705 were in most positions, and at and in B*1403 and B*2705 was for B*1403. P3 and and were in B*1403. and and were in B*1403. at a of in B*1403 and in B*2705 was A comparison between the B*1402 and the B*2705 ligands a of with as the of statistical in residue usage at P3 and disparity in residue usage at multiple the peptide sharing observed between B*1402 B*1403 and B*2705. be that are at among B*1402 and B*1403 ligands and positions, in B*2705 this the of the and peptide to and that HLA-B14 ligands were by The of peptide with residue to other HLA class I was for B*1402 M. J. J. Full Text PDF PubMed Google differences in residue usage between B*1402, B*1403, and B*2705-bound different of with different usage between and B*2705-bound nonamers. and the are in different of with different usage between and B*2705-bound nonamers. and the are in to the B*2705 and the comparison to the B*2705 and the comparison not of with different usage between and B*2705-bound nonamers. and the are in to the B*2705 and the comparison not in a with B*1402 and ligands of B*1403 and B*2705 were were shared between B*1402 and B*1403. shared by B*1403 and but absent in B*1402 were by in this two not in B*1403 were as B*2705 were from B*2705 in this and as a ligand of B*2705 and de Castro J.A. Alvarez I. Marcilla M. Paradela A. Ramos M. Sesma L. Vazquez M. Tissue Antigens. 2004; 63: 424-445Crossref PubMed Scopus (85) Google Scholar). A of the shared ligands in is in of and P3 and ligands shared between HLA-B27 and and 7Lopez de Castro J.A. Alvarez I. Marcilla M. Paradela A. Ramos M. Sesma L. Vazquez M. Tissue Antigens. 2004; 63: 424-445Crossref PubMed Scopus (85) Google de Castro J.A. Alvarez I. Marcilla M. Paradela A. Ramos M. Sesma L. Vazquez M. Tissue Antigens. 2004; 63: 424-445Crossref PubMed Scopus (85) Google and 7Lopez de Castro J.A. Alvarez I. Marcilla M. Paradela A. Ramos M. Sesma L. Vazquez M. Tissue Antigens. 2004; 63: 424-445Crossref PubMed Scopus (85) Google de Castro J.A. Alvarez I. Marcilla M. Paradela A. Ramos M. Sesma L. Vazquez M. Tissue Antigens. 2004; 63: 424-445Crossref PubMed Scopus (85) Google de Castro J.A. Alvarez I. Marcilla M. Paradela A. Ramos M. Sesma L. Vazquez M. Tissue Antigens. 2004; 63: 424-445Crossref PubMed Scopus (85) Google in a Alloreactive among B*1402, B*1403, and B*2705 are by Immunol. PubMed Scopus Google Scholar). This is due to the that the clones a of the bound to the molecule A. 1991; PubMed Scopus Google Scholar, J. Med. 1991; PubMed Scopus Google Scholar, J. Immunol. Google Scholar). the of to analyze the shared antigenic features of as a of their constitutive peptide repertoires. A of clones against B*1402 from various were for their to The specificity of the clones was from their lack of of and their of was as the of B*1403 to the of were considered to indicate lack of was considered as of the of were considered as a epitope as a of of the of the clones with B*1403, with among This percentage was only the percentage of peptide between B*1402 and B*1403 these constitutive these results of the shared ligands between B*1402 and B*1403 maintain their antigenic by a when bound to both among B*1402, B*1403 and B*2705 with with cross-reactive with HLA class I of the are as and of with cross-reactive with of The HLA class I of the are as and in a A was to analyze epitope sharing between HLA-B14 and B*2705. this clones against B*1402 for of not be to be used as were not and to as were a of from only both from the with B*2705. This percentage was to the peptide sharing between B*1403 and when the between both by was for the percentage of shared as by of in an peptide between B*1403 and B*2705 of to Although a was not with B*1402, is to that the be their peptide sharing by was to the The two that with B*2705 and with B*1403, suggesting that shared by B*1402 and but absent in B*1403. with features were in this and clones from various against B*2705 were for of B*1402 and B*1403, of these the not the peptide is that the of was not to with The B*1402 and B*1403 subtypes a disparity in their constitutive peptide repertoires that was in of their with only an L156R and which from other only by the of their peptide repertoires L. L. R. L. J. J. J. Med. PubMed Scopus Google Scholar). at residue peptide specificity at two by peptide this residue in the and of the which the P3 and D.R. Wiley D.C. Full Text PDF PubMed Scopus Google Scholar, Wiley D.C. Nature. PubMed Scopus Google Scholar). by peptide with the was to the with the associated with antigen processing which is mediated by the J. J.A. R. J. P. PubMed Scopus Google Scholar), on the basis of the different binding of and N. M. Tissue Antigens. PubMed Scopus Google Scholar, A. R. J. J. Immunol. Google Scholar). This mechanism is not by the peptide sharing between the two subtypes L. L. R. L. J. J. J. Med. PubMed Scopus Google Scholar), but not a different effect of the on peptide the change at in these subtypes is Although with the were not in this the peptide differences between B*1402 and B*1403 can be explained to a by an effect of residue on specificity. differences in residue usage among bound were at two of P3 and P7, in the of which residue is an The for at both in B*1402 and for and at P3 and P7, in B*1403 are with the in B*1402 and the in B*1403. The basis for the of B*1403 for is not in the of an from in and in the of residue the binding and of B*1402, were to be by the presence of M. J. J. Full Text PDF PubMed Google Scholar). of B*1403 for this of was from the of although not statistical This is not explained by a direct effect of B*1402 and B*1403 the A including the is that of residue on to the A pocket residue specificity between B*1402 and B*1403, but this can only be by the of B*1403 for of this with P3 are among the most for binding J. A. J. Med. PubMed Scopus Google Scholar, J. J. Immunol. Google Scholar, N. L. J. J. Immunol. Google Scholar, R. 2002; PubMed Scopus Google Scholar). the in this at both and and but one these of in at one of these results two A is that B*1403 with in the and is B*1402 for with A is that the for P3 from a direct of on pocket to binding for peptide binding of that of B*1403 with other of the This can be by direct of these which was not in this class I ligands the as and are to J. R. N. Nature. 2002; PubMed Scopus Google Scholar, J.A. Immunol. 2002; PubMed Scopus Google Scholar), the relationship between of HLA class I ligands and of the allotype is not However, is that one of the shared ligands among B*1402, B*1403, and which from the peptide of is a as by from the B*2705-bound peptide from the Ramos and J. A. de the and differences between the and peptide repertoires are largely explained by the of residue on at two of the bound although on be formally of other differences between these two which to be as with the to the to that the differences between their peptide for the that the association of B*1402 and B*1403 to be to their peptide as proposed by the arthritogenic peptide hypothesis in Scholar). an of disparity from distinct of shared ligands by these two as observed in L. L. R. L. J. J. J. Med. PubMed Scopus Google Scholar). this used clones as to analyze epitope sharing between B*1402 and B*1403. This was on that constitutive A. 1991; PubMed Scopus Google Scholar, J. Med. 1991; PubMed Scopus Google Scholar, J. Immunol. Google Scholar). that the of is due to of a of bound to the molecule, that a different peptide A. 1991; PubMed Scopus Google Scholar, J. Immunol. Google Scholar). This is the of the clones are against one peptides. although can with distinct among other J. Full Text PDF PubMed Scopus Google Scholar), is to that between closely with a of peptide sharing be on of shared This is to in the peptide by any is However, was formally for HLA-B27 subtypes in at one A. M. Vazquez J. Lopez de Castro J.A. J. Immunol. Google Scholar). at shared ligands of B*2705 and a when bound to both R.A. A. J. 2004; Full Text Full Text PDF PubMed Scopus Google Scholar, M. R. A. J. Mol. PubMed Scopus Google Scholar). the that the percentage of clones between B*1402 and B*1403 closely peptide that most of the shared ligands maintain their antigenic and a when bound to Our results with of HLA-B14 subtypes are different from those for and this the change a effect on peptide and a one on L. L. R. L. J. J. J. Med. PubMed Scopus Google Scholar). A different in the of HLA-B14 has on peptide but to effect on of shared the of in a be on the nature of the the molecular in which and which by only the L156R a shared peptide epitope with a but and T-cell of this epitope was due to an effect of this on the of the L. J. J. J. Full Text Full Text PDF PubMed Scopus Google Scholar). susceptibility to were on T-cell of specific as proposed by the arthritogenic peptide hypothesis (5Benjamin R. Parham P. Immunol. Today. 1990; 11: 137-142Abstract Full Text PDF PubMed Scopus (350) Google Scholar), one would to shared ligands and common peptide features between the disease-associated B*2705 and B*1403. The of shared ligands between these two was formally in this However, is that sharing common ligands with HLA-B27 by that the allotype to This is by the lack of association of and with this their peptide sharing with subtypes L. A. Vazquez J. Lopez de Castro J.A. J. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar, M. Paradela A. Vazquez M. A. Vazquez J. Lopez de Castro J.A. J. 2002; Full Text Full Text PDF PubMed Scopus Google and, in this by of ligands shared by B*2705 and the of shared was that T-cell between B*1402 and B*2705 be and that the percentage of cross-reactive clones was with the peptide sharing between B*1402 B*1403 and B*2705. of the differences between HLA-B27 and of the shared ligands maintain their features on both allotypes. these of distinct on but this would that different ligands of HLA-B27 and HLA-B14 antigenic their with their Although were not to that a of between B*1403 and B*2705. The of shared ligands and cross-reactive clones between HLA-B27 and HLA-B14 that B*1403 and B*2705 present shared with the antigenic features distinct antigenic This is a of the arthritogenic peptide hypothesis (5Benjamin R. Parham P. Immunol. Today. 1990; 11: 137-142Abstract Full Text PDF PubMed Scopus (350) Google Scholar). However, results are on which are to and of antigenic mimicry between B*1403 and B*2705 ligands would with other be shared by B*1403 and but absent in B*1402, were found. Although results do the of be the basis for the differences between the and B*2705-bound peptide repertoires are explained by the distinct of the peptide ligands at multiple positions, and by the that for one allotype are not among ligands of the do not the of a common peptide presented by B*1403 and but not by B*1402, but that the of a peptide be has and between two HLA class I associated with that to the of this as of specific peptides. However, molecular among peptide repertoires and the of although as for the antigenic of shared ligands bound to different are to a direct to the mechanism of the pathogenetic features of HLA-B27 and B*1403 to be studies in and P. de and de and their for in and for their
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