Expression and immunogenicity of the entire human T cell leukaemia virus type I envelope protein produced in a baculovirus system.

The entire envelope gene of human T cell leukaemia virus type I (HTLV-I) has been successfully expressed in a baculovirus non-fusion vector system. The HTLV-I envelope protein accumulated within the insect cells as inclusion bodies which allowed efficient recovery of the recombinant protein. In an attempt to study the role of the HTLV-I envelope glycoprotein as an immunogenic target, mice were immunized with the envelope protein inclusion bodies (env-I.B.) in the presence or absence of an adjuvant. Antibodies of broad specificity were produced against the HTLV-I envelope protein in the presence or absence of an adjuvant as detected by Western blotting, radioimmunoprecipitation and peptide ELISA. Neutralizing antibody was detected when env-I.B. immunizations were carried out in the presence of high doses of a new adjuvant composed of a mycobacterial cell wall extract. In a combined immunization regimen, env-I.B. were found to enhance and broaden the antibody response to the HTLV-I envelope glycoprotein, following priming with various recombinant vaccinia virus (RVV) constructs expressing either the entire native HTLV-I envelope (gp46 and gp21) or just the surface envelope protein (gp46). Increased titres of neutralizing antibodies were observed following priming with the RVV expressing gp46 only. Results indicate that immunization regimens that involve priming with RVV expressing HTLV-I envelope followed by boosting with recombinant baculoviral HTLV-I envelope might be useful in eliciting protective immune responses in vivo.