Enhanced Immunogenicity of Recombinant and Synthetic Peptide Vaccines

In an attempt to produce more stable and defined vaccines, scientists have been studying the immune responses to many infectious agents in detail in order to identify the critical epitopes involved in providing protective immunity. Armed with this knowledge, it is now possible to mimic such epitopes by producing short peptides and to use these as the basis of a vaccine (Francis, 1990). However, once a vaccine candidate peptide has been identified or predicted then it must be delivered to the immune system in a suitable manner in order to elicit not just a high titre anti-peptide response but anti-peptide antibodies that will recognise and neutralize the infectious agent. Indeed, there has been a widely held view that, due to their relatively small molecular size, peptides are necessarily poor immunogens and thus require carrier-coupling to enhance their immunogenicity. As a result of this there are many examples of elegantly defined peptides which, having been coupled in an uncontrolled manner to large undefined carrier proteins, produced anti-peptide antibodies that totally failed to recognise the native protein. These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.