Production of a recombinant human T‐cell leukemia virus type‐I trans‐activator (tax1) antigen and its utilization for generation of monoclonal antibodies against various epitopes on the tax1 antigen

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Abstract
A 42-kDa recombinant protein, PX141, consisting of the trans-activator protein encoded by human T-cell leukemia virus (HTLV-I) (tax, antigen) and the amino-terminal fusion peptide of 12 amino acid residues of the a-peptide encoded by the plasmid pUC19 was produced. In order to investigate the immunogenicity of the tax, antigen, mice were immunized with the purified PX141 and 4 anti-tax, monoclonal antibodies (MAbs) designated TAXY-I, TAXY-6, TAXY-7 and TAXY-8 were generated, and their reactivity was characterized along with another anti-tax, MAb, Lt-4. Immunoblot assays showed that all the MAbs reacted with the PX141, the native tax, antigen expressed in various HTLV-I-infected cell lines and the gp68 of MT-2 cells expressing the tax, amino acids 94–353. Immunoblot assays using recombinant, truncated tax, antigens, XD59 (expressing amino acids 180–338) and XD128 (expressing amino acids 1–47 and 286–353) showed that: (I) TAXY-I and Lt-4 did not react with either antigen; (2) TAXY-6 and TAXY-8 reacted with only XD128; and (3) TAXY-7 reacted with both. In addition, TAXY-I, but not the other MAbs, reacted with a putative tax antigen of an STLV-I-infected cell line, designated RfM26-I. Competitive binding assays showed that TAXY-6 and TAXY-8 did not compete against each other. Sera from HTLV-I-infected humans interfered with the binding of all of these anti-tax, MAbs. These results indicate that the tax1 antigen and the PX141 express at least 5 distinct epitopes recognized by human and mouse antibodies.

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