Baculovirus expression of antibodies: A method for the expression of complete immunoglobulins in a eukaryotic host

Abstract

To express complete immunoglobulin heterodimers in vitro, we have taken advantage of the baculovirus expression system. Several approaches to the simultaneous expression of recombinant heavy and light chains were examined, including coinfection with separate γ and κ expressing viruses, as well as infection with a single double recombinant virus that expresses both polypeptides. In both cases, the antibodies produced were correctly processed, glycosylated, and assembled into normal immunoglobulin heterodimers. Furthermore, the antibodies recovered from the supernatants of infected cultures behaved indistinguishably from B-cell-derived immunoglobulins with similar specificities. An additional benefit of a baculovirus-based expression system is the high yield of recombinant material produced in insect cells. Thus we describe here a general method for the high-level expression of authentic antibodies in a eukaryotic host.