» Articles » PMID: 3260607

Molecular Characterization of Human Ro/SS-A Antigen. Amino Terminal Sequence of the Protein Moiety of Human Ro/SS-A Antigen and Immunological Activity of a Corresponding Synthetic Peptide

Overview
Journal J Clin Invest
Specialty General Medicine
Date 1988 Jul 1
PMID 3260607
Citations 28
Authors
Affiliations
Soon will be listed here.
Abstract

The Ro/SS-A antigen was purified from an Epstein-Barr virus-transformed human B lymphoblastoid cell line. The amino terminal amino acid sequence of the 60-kD polypeptide bearing this antigenic epitope was determined to be: (formula; see text) A peptide composed of residue 6-19 was synthesized by the solid-phase method. Immunodiffusion-defined monospecific autoimmune sera to Ro/SS-A reacted with this synthetic peptide in ELISA, whereas autoantibodies with other specificities such as anti-La/SS-B and anti-Sm, as well as normal human sera, were not reactive. In addition, rabbit anti-peptide 6-19 antisera reacted specifically with native human Ro/SS-A antigen in ELISA. Furthermore, this synthetic peptide inhibited the binding of rabbit anti-peptide antiserum to native human Ro/SS-A. An additional synthetic peptide corresponding to residues 7-24 partially inhibited the binding of a patient anti-Ro/SS-A serum to native Ro/SS-A. These results suggest that the amino terminal portion of the molecule represents a major epitope of Ro/SS-A. The determination of the amino acid sequence of Ro/SS-A and the availability of synthetic peptide(s) bearing this antigen should provide additional approaches to further characterize the autoimmune response to this antigen.

Citing Articles

Calreticulin binds preferentially with B cell linear epitopes of Ro60 kD autoantigen, enhancing recognition by anti-Ro60 kD autoantibodies.

Staikou E, Routsias J, Makri A, Terzoglou A, Sakarellos-Daitsiotis M, Sakarellos C Clin Exp Immunol. 2003; 134(1):143-50.

PMID: 12974767 PMC: 1808837. DOI: 10.1046/j.1365-2249.2003.02246.x.


Fine specificity of autoantibodies to calreticulin: epitope mapping and characterization.

Eggleton P, Ward F, Johnson S, Khamashta M, Hughes G, Hajela V Clin Exp Immunol. 2000; 120(2):384-91.

PMID: 10792392 PMC: 1905652. DOI: 10.1046/j.1365-2249.2000.01214.x.


Release of calreticulin from neutrophils may alter C1q-mediated immune functions.

Kishore U, Sontheimer R, Sastry K, Zaner K, Zappi E, Hughes G Biochem J. 1997; 322 ( Pt 2):543-50.

PMID: 9065775 PMC: 1218224. DOI: 10.1042/bj3220543.


Constitutive expression of calreticulin in osteoblasts inhibits mineralization.

St-Arnaud R, Prudhomme J, Dedhar S J Cell Biol. 1995; 131(5):1351-9.

PMID: 8522595 PMC: 2120639. DOI: 10.1083/jcb.131.5.1351.


Structure and homology of human C1q receptor (collectin receptor).

Malhotra R, Willis A, Jensenius J, Jackson J, Sim R Immunology. 1993; 78(3):341-8.

PMID: 8478019 PMC: 1421832.


References
1.
Getzoff E, Geysen H, Rodda S, Alexander H, Tainer J, Lerner R . Mechanisms of antibody binding to a protein. Science. 1987; 235(4793):1191-6. DOI: 10.1126/science.3823879. View

2.
Geysen H, Tainer J, Rodda S, Mason T, Alexander H, Getzoff E . Chemistry of antibody binding to a protein. Science. 1987; 235(4793):1184-90. DOI: 10.1126/science.3823878. View

3.
Bixler Jr G, Bean M, Atassi M . Site recognition by protein-primed T cells shows a non-specific peptide size requirement beyond the essential residues of the site. Demonstration by defining an immunodominant T site in myoglobin. Biochem J. 1986; 240(1):139-46. PMC: 1147386. DOI: 10.1042/bj2400139. View

4.
Lieu T, Reimer C, Sontheimer R . Immunoglobulin class and subclass profile of the Ro/SS-A autoantibody response. J Invest Dermatol. 1988; 90(2):158-64. DOI: 10.1111/1523-1747.ep12462142. View

5.
Clark G, Reichlin M, TOMASI Jr T . Characterization of a soluble cytoplasmic antigen reactive with sera from patients with systemic lupus erythmatosus. J Immunol. 1969; 102(1):117-22. View