Abstract
The development of selective anticancer vaccines that provide enhanced protection against tumor recurrence and metastasis has been the subject of intense research in the scientific community. The tumor-associated glycoprotein MUC1 represents a well-established target for cancer immunotherapy and has been used for the construction of various synthetic vaccine candidates. However, many of these vaccine prototypes suffer from an inherent low immunogenicity and are susceptible to rapid in vivo degradation. To overcome these drawbacks, novel fluorinated MUC1 glycopeptide-BSA/TTox conjugate vaccines have been prepared. Immunization of mice with the 4’F-TF-MUC1-TTox conjugate resulted in strong immune responses overriding the natural tolerance against MUC1 and producing selective IgG antibodies that are cross-reactive with native MUC1 epitopes on MCF-7 human cancer cells.
Highlights
Since cancer has advanced to one of the leading causes of death in economical developed countries, the search for novel anticancer therapies is of high current interest
To allow for the use of vaccines derived from TACA analogs without metabolic cell glycoengineering, the structural integrity of the saccharide epitope must be maintained and cross-reactivity of the elicited antibodies with the native tumor-associated glycans is required
Yang et al found that fluorinated sTn antigen conjugates were significantly more immunogenic than their natural congeners and elicited antibodies cross-reactive to sTn-positive LS-C tumor cells [32]. In this context and as part of ongoing research devoted to the development of selectively fluorinated MUC1 glycopeptide-based vaccines, we report on the successful preparation of two novel MUC1 glycoconjugates comprising 4’-deoxy-4’-fluoro-TF antigen side chains in their B cell epitopes
Summary
Since cancer has advanced to one of the leading causes of death in economical developed countries, the search for novel anticancer therapies is of high current interest. To allow for the use of vaccines derived from TACA analogs without metabolic cell glycoengineering, the structural integrity of the saccharide epitope must be maintained and cross-reactivity of the elicited antibodies with the native tumor-associated glycans is required.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have