Epstein-Barr virus nuclear antigen (EBNA): antigenicity of the molecule encoded by the BamH1 K fragment of the EBV genome
The major antigenic component of the Epstein-Barr virus nuclear antigen complex (EBNA) is a highly polymorphic (69–94K mol. wt.) polypeptide. Its molecular weight correlates with the size of the large Hind III subfragment of the BamH1 K fragment of the EBV genome which contains the third internal repeat region, IR3.
The region of the molecule encoded by IR3, plus a small number of flanking residues, forms a large peptide fragment which the amino acid sequence predicts is trypsin resistant. Immunoblotting of trypsin digested, partially purified, BamH1 K encoded EBNA (BK EBNA) from various cell lines demonstrates that this region is antigenic and shows it must be an immunogenic determinant in the native molecule. It also confirms that it is responsible for the size polymorphism. Immunoblotting other peptide fragments with a variety of sera show that different epitopes on BK EBNA. The possibility that anti-RANA (Rheumatoid Arthritis Associated Nuclear Antigen) might represent a specific component of anti-EBNA antisera is considered.
KeywordsNuclear Antigen Repeat Array Native Molecule Immunogenic Determinant Trypsin Cleavage
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