Identification of antigenic regions of the human Ro 60 kDa protein using recombinant antigen and synthetic peptides

Wahren, Marie; Rudén, Ulla; Andersson, Birger; Ringertz, Nils R.; Pettersson, Ingvar

doi:10.1016/0896-8411(92)90146-h

Cited by 51 publications

(47 citation statements)

References 26 publications

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“…Theconformalion of R06O has also been shown to he very important tor RNA recognition (23]-Our finding does of course not exclude the possibility thai linear epitopes on R06O can be recognized by a minority of antibody molecules in anti-Ro sera, as indeed has been shown by Scofield & Harley [29], Wahren and eoworkers [13], and Barakai and coworkers [14].…”

Section: Epitope Recognition Patterns Of Ro6fl and Ro52supporting

confidence: 60%

“…Wahren and coworkers [13] have identified antigenic regions of human Ro60 using recombinant antigen and synthetic pcplides using IB. They also ohserved heterogeneity in the autoimmune response to Ro60, A recent report by Barakat and coworkers [14] showed that antibodies from patients with primary Sjogren's .syndrome (pSS)jnti SLE might recognize differenl linear epitopes on Ro60.…”

Section: Introductionmentioning

confidence: 99%

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Sera from patients with rheumatic diseases recognize different epitope regions on the 52-kD Ro/SS-A protein

Božič

Pruijn

Rozman

et al. 1993

Clinical and Experimental Immunology

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SUMMARYPatients suffering from systemic lupus erythematosus (SLE) or Sjogren's syndrome (SS) often contain autoantibodies directed to the Ro(SS-A) complex. In this study the antigenic determinants on two of the components of the Ro complex, i.e. the Ro60 and the Ro52 polypeptides. were investigated. Anti-Ro* sera were selected by counter-immunoelectrophoresis. Depending on the detection method. 59-68% of the SLE patients produced anti-Ro but not anti-La anlibody. while 72-81'%. ofthe SS patients produced both anti-Ro and anti-La antibody, Immunoprecipitation of recombinant Ro-protcins showed that 61 sera (87"/i) were reactive with both Ro proteins, seven sera with Ro60 only, one serum with Ro52 only, and one serum did not precipitate the proteins at all. The anti-Ro60 reactivity of human sera is strongly associated with the native form of Ro60. suggesting that conformational autoepitopes are an important feature of Ro60. In the case of Ro52, frequently the residues located between amino acids 216 and 292 were essential for reactivity with the antibodies. With 70% ofthe lupus sera tested this appeared to be the only region important for reactivity. The antibodies of SS patients generally recognized multiple B cell epitopes located between amino acids 55 and 292. The results of this study indicate that the antigenic determinants on Ro52 are different for autoantibodies produced by lupus patients compared with those of SS patients.

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Section: Epitope Recognition Patterns Of Ro6fl and Ro52supporting

confidence: 60%

Section: Introductionmentioning

confidence: 99%

Sera from patients with rheumatic diseases recognize different epitope regions on the 52-kD Ro/SS-A protein

Božič

Pruijn

Rozman

et al. 1993

Clinical and Experimental Immunology

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“…Later on, Barakat et al [16] using five selected synthetic peptides revealed an oligopeptide (21-41) with considerable reactivity with anti-Ro/SSA sera [16]. Wahren et al [17] using recombinant fusion protein of 60-kD Ro/SSA has shown that all anti-Ro/SSA sera recognized an epitope in the central region 181-396. Routsias et al [18] using 22-mer, synthetic peptides overlapping by 8 residues covering the entire sequence of the 60-kD Ro/SSA autoantigen, revealed two disease-specific epitopes: the TKYKQR-NGWSHKDLLRSHLKP (169-190) and the ELYKE-KALSVETEKLLKYLEAV (211-232) region recognized by sera from SLE and SS patients, respectively ( fig.…”

Section: Structure Of Autoantigensmentioning

confidence: 99%

Sjögren’s Syndrome: Autoantibodies to Cellular Antigens

Mavragani

Tzioufas

Moutsopoulos³

2000

Int Arch Allergy Immunol

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Autoantibodies to cellular autoantigens are usually found in sera of patients with systemic autoimmune rheumatic diseases. Patients with Sjögren’s syndrome (SS) frequently present autoantibodies to both organ and non-organ-specific autoantigens. The most commonly detected autoantibodies are those directed against the ribonucleoproteins Ro/SSA and La/SSB. The presence of the antibodies in SS is associated with early disease onset, longer disease duration, parotid gland enlargement, higher frequency of extraglandular manifestations and more intense lymphocytic infiltration of the minor salivary glands. Over the past several years, the structure and function of these autoantigens have been extensively studied. Several centers, using different techniques, have investigated the B cell epitopes on the protein components Ro 60 kD, Ro 52kD, and La 48 kD. Finally, increased evidence of direct involvement of anti-Ro/SSA and anti-La/SSB autoantibodies in the pathogenesis of tissue injury has been contributed by several studies.

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“…Some epitopes recognized by the anti-Ro/SS-A MoAbs are comparable to those recognized by sera of patients. Although the epitope of MoAb IDS (aa531-aa538) was not found to be a major autoantigenic region [44 46], the epitope recognized by MoAb 2GI0 (aa232 aa236) exactly matches a highly autoantigenic region in the 60-kD Ro/SS-A molecule recognized by sera of several patients [44,47]. Since it is possible to predict antigenic regions in a protein molecule on the basis of amino acid sequences [48].…”

Section: Discussionmentioning

confidence: 99%

Characterization of murine monoclonal antibodies against 60-kD Ro/SS-A and La/SS-B autoantigens

Veldhoven

Pruijn

Meilof

et al. 1995

Clinical and Experimental Immunology

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SUMMARY Small cytoplasmic ribonucleoproteins (scRNPs) are important autoantigens in patients with systemic lupus erythematosus and Sjögren's syndrome. MoAbs against these proteins were made by immunization of BALB/c mice with purified human recombinant 60‐kD Ro/SS‐A or 50‐kD La/SS‐B proteins. Five stable hybridoma cell lines were obtained, of which four secreted anti‐Ro/SS‐A antibodies (clones 1D8, 1D11, 2G10 and 6G8) and one produced anti‐La/SS‐B antibodies (clone 7F6). The MoAbs were further characterized using four different immunoassays: immunofluorescence, immunoblotting, RNA precipitation combined with Northern blotting, and recombinant protein precipitation. All lour MoAbs against Ro/SS‐A recognized the native protein and one of them (2G10) recognized also intact scRNP particles. Interestingly, hY3‐RNA was reproducibly not efficiently precipitated by MoAb 2G10. Epitope mapping using deletion mutants of the 60‐kD Ro/SS‐A antigen showed that MoAb ID8 recognized the C‐terminal part of this protein, while 1D11 and 2G10 recognized distinct epitopes in the region between the RNP motif and the putative zinc finger domain. The epitopes recognized by these MoAbs lire highly conserved among species, and the epitope recognized by MoAb 2G10 may be identical to an autoepitope recognized by sera of patients. This is the first report describing the isolation and characterization of MoAbs of the IgG class against the 60‐kD Ro/SS‐A and La/SS‐B autoantigens obtained by immunization with purified human recombinant proteins. These MoAbs can be of great use in studying the cellular processes in which scRNPs are involved, and may help to determine why these scRNPs become autoantigenic in autoimmune diseases.

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Identification of antigenic regions of the human Ro 60 kDa protein using recombinant antigen and synthetic peptides

Cited by 51 publications

References 26 publications

Sera from patients with rheumatic diseases recognize different epitope regions on the 52-kD Ro/SS-A protein

Sera from patients with rheumatic diseases recognize different epitope regions on the 52-kD Ro/SS-A protein

Sjögren’s Syndrome: Autoantibodies to Cellular Antigens

Characterization of murine monoclonal antibodies against 60-kD Ro/SS-A and La/SS-B autoantigens

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