A synthetic peptide-based polyoxime vaccine construct of high purity and activity.

An artificial protein containing four copies of a peptide comprising the C-terminal 23 residues of influenza virus hemagglutinin was constructed using oxime chemistry and compared with two tetrameric multiple antigenic peptide (MAP) constructions of the same peptide displayed either radially or linearly which were made by conventional techniques. The tetra-oxime was much more homogeneous yielding a single peak on reversed phase HLPC and the correct mass spectrum. In addition, the tetra-oxime was found to be recognized by anti-peptide antibodies, to stimulate at low concentrations a T-cell clone and also to elicit in mice high titres of antibodies which were able to recognize native virus. The modular polyoxime approach, which permits artificial proteins to be assembled rapidly, in high yield and in high purity, is expected to lead to an increase in the use of artificial proteins in vaccine technology.