Secretion and processing of an immunoglobulin light chain in Escherichia coli.

When a cDNA coding for the kappa light chain (L-321) from the mouse MOPC321 myeloma was cloned into Escherichia coli, L-321 antigens were found in both cytoplasmic and periplasmic fractions. In cells synthesizing the intact chain, starting with its signal peptide, the periplasm contained a mature-size immunoglobulin indicating that the eukaryotic signal peptide can initiate secretion and be processed. When the entire cDNA for L-321 (including its signal peptide) was inserted in the gene for bacterial beta-lactamase, processing cleaved only the first bacterial signal sequence of the hybrid protein synthesized. Removal of the beta-lactamase signal peptide was also observed with another beta-lactamase-L-321 hybrid which did not include the immunoglobulin signal peptide and the adjacent part of the variable region. The two hybrid proteins may, however, differ in their mode of secretion.