A Charged Segment Mainly Composed of Basic Amino Acids Forms an Autoepitope of CENP-A

Muro, Yoshinao; Iwai, Teruki; Ohashi, Masaru

doi:10.1006/clin.1996.0013

Cited by 12 publications

(19 citation statements)

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“…They also suggested that a possibly more generally conserved feature of the autoantigens consists of extended surface structures that are charge-, proline-, or glycinerich. In our previous study [17] we focused on the characteristic amino acid sequences in CENP-A and synthesized peptides composed of amino acid residues 3±17 (named peptide A in this study). That region contains 7 Arg (R), 1 Lys, and 3 Pro (P), and two repeats of PRRRS.…”

Section: Discussionmentioning

confidence: 99%

“…ELISA ELISA was performed basically according to the published protocol [17]. Nunc microtitre wells were coated with 50 ng of the synthetic peptides conjugated to BSA (0´5 mg/ml in PBS) at 48C overnight.…”

Section: Synthetic Peptidesmentioning

confidence: 99%

“…Following incubation for 1 h with shaking at room temperature, the wells were washed three times with PBS±T and twice with PBS. After a 1-h incubation with the substrate solution [17] at room temperature, absorbance (405 nm) was determined with a 340 ATTC (Tecan Co., Salzberg, Austria). The absorbance with the synthetic peptides following subtraction of the antibody reactivity to BSA was the value for each individual.…”

Section: Synthetic Peptidesmentioning

confidence: 99%

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Autoepitopes on autoantigen centromere protein-A (CENP-A) are restricted to the N-terminal region, which has no homology with histone H3

Muro

Azuma²,

Onouchi³

et al. 2000

Clinical and Experimental Immunology

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SUMMARYAnti-centromere autoantibodies (ACA) are commonly found in the serum of patients with a limited type of scleroderma and other systemic autoimmune diseases. CENP-A is one of the major antigens against ACA and a histone H3-like protein. To analyse the autoantigenic epitopes of CENP-A, a series of truncated peptides of human CENP-A were expressed in Escherichia coli and immunoblotting analysis was performed with 91 ACA 1 sera. Eighty sera (88%) with the ACA reacted to the 52-amino acids N-terminal region which is not homologous to H3, while no sera reacted to the C-terminus which has a sequence similarity with H3. Moreover, ELISA was also employed in this study using two synthetic peptides corresponding to the amino acid sequences 3±17 (peptide A) and 25±38 (peptide B). Peptides A and B were reactive to 78 (86%) and 79 (87%) of ACA, respectively. Core antigens of hepatitis B virus (HBV) and hepatitis C virus (HCV) have similar sequences to peptide A and/or peptide B, but three sera containing HBV without ACA and five sera containing HCV without ACA were found to be reactive to neither peptide. Centromere localization of CENP-A is dependent on the H3-like C-terminal domain which is not autoantigenic, while the antigenic N-terminal domain, which might play unidentified functional roles, should be an important region for the induction of ACA.

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Section: Discussionmentioning

confidence: 99%

Section: Synthetic Peptidesmentioning

confidence: 99%

Section: Synthetic Peptidesmentioning

confidence: 99%

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Autoepitopes on autoantigen centromere protein-A (CENP-A) are restricted to the N-terminal region, which has no homology with histone H3

Muro

Azuma²,

Onouchi³

et al. 2000

Clinical and Experimental Immunology

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“…Rather, three peptide sequences were arbitrarily chosen for detailed study by one or more groups of investigators [36][37][38], leaving 60% of the protein yet to be characterized. However, the first report of a specific peptide epitope (residues 3-17) [36] was characteristic of the autoantigen prototype described by Brendel et al [39] a highly charged array containing repeated sequences. This N-terminal peptide appears to be a significant target of ACA [36,38].…”

Section: Discussionmentioning

confidence: 99%

“…However, the first report of a specific peptide epitope (residues 3-17) [36] was characteristic of the autoantigen prototype described by Brendel et al [39] a highly charged array containing repeated sequences. This N-terminal peptide appears to be a significant target of ACA [36,38]. The identification of this immunoreactive domain also facilitated study of CENP-A conservation.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Comparison of Natural and Recombinant Human CENP-A Autoantigen

Martı́nez

Sun

Billings

et al. 1998

Journal of Autoimmunity

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Development of a CENP‐A/CENP‐B–specific immune response in a patient with systemic sclerosis

Mähler¹,

Mierau²,

Genth³

et al. 2002

Arthritis & Rheumatism

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Antibodies directed against an epitope motif on CENP‐A have been shown to cross‐react with mimotopes on other autoantigens and on Epstein‐Barr nuclear antigen 1 (EBNA‐1), suggesting a molecular mimicry. We describe here the gradual development of an anticentromere immune response in a patient with systemic sclerosis, which started from an antihistone response and was not mediated by molecular mimicry. Via an epitope on histone H3, the antibody response spread to a homologous epitope in the H3 homology domain of CENP‐A. This was followed by an intramolecular epitope spreading to N‐terminal peptides of CENP‐A containing the known epitope motif G‐P‐X1‐R‐X2. From there it spread to corresponding epitopes on CENP‐B and to mimotopes of the major CENP‐A epitope motif on other autoantigens including EBNA‐1. Whether the D‐penicillamine treatment received by this patient was involved in the triggering of this cascade remains a matter of speculation.

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A Charged Segment Mainly Composed of Basic Amino Acids Forms an Autoepitope of CENP-A

Cited by 12 publications

References 0 publications

Autoepitopes on autoantigen centromere protein-A (CENP-A) are restricted to the N-terminal region, which has no homology with histone H3

Autoepitopes on autoantigen centromere protein-A (CENP-A) are restricted to the N-terminal region, which has no homology with histone H3

Isolation and Comparison of Natural and Recombinant Human CENP-A Autoantigen

Development of a CENP‐A/CENP‐B–specific immune response in a patient with systemic sclerosis

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