© ELSEVIER Paris 1987 LETTERS TO THE EDITOR Ann. Inst. Pasteur/Viral. 1987, 138,273-278 SYNTHETIC PEPTIDES AS VIRUS VACCINES: RECOMBINANT SUBUNIT VACCINES by P.W. Berman Department of Molecular Biology, Genentech, Inc., 460 Point San Bruno Boulevard, South San Francisco, CA 94080 (USA) I. - Introduction. II. - Expression of viral surface pro- teins in E. coli. In the last decade, at least four imaginative strategies have been descri- bed for the production of human vac- cines. These include recombinant subunit vaccines, synthetic peptide vac- cines, recombinant virus (e.g. vaccinia virus) vaccines and anti-idiotype vac- cines. Perhaps the most significant feature common to all of these ap- proaches is that they eliminate the need for the large-scale cultivation of the pathogenic organism against which the vaccine is directed . Rather. they work by providing molecular facsimiles of the major neutralizing antigenic deter- minants. Because other Forum papers have considered synthetic peptide vac- cines, this discussion will be limited to subunit vaccines produced by recombi- nant DNA technology. Received October 18, 1986. In the late 1970's, it became clear that E. coli or other microorganisms could be genetically programmed to synthesize virtually any polypeptide. What was not clear, however, was whether recombinant polypeptides pro- duced in these organisms could duplicate the unique three-dimensional conformation essential for biological activity or immunological identity. Although E. coli has now been used suc- cessfully to produce a wide variety of eukaryotic enzymes and hormones, there are few examples of efficacious vaccine products produced in this bacteria. There are several factors which can account for the lack of success of E. coli as a substrate for vaccine production. Because full-length viral This paper was originally scheduled for publication in the Forum which appeared in thc Annales de I'Institut Pasteur /Virology, 1986, 137 E, n° 4.