Purification, preparation, and use of chaperone-peptide complexes for tumor immunotherapy

Abstract

The molecular chaperone heat-shock protein 70 (Hsp70) possesses immune stimulatory properties that have been employed in the preparation of anticancer vaccines. Hsp70 binds antigenic peptides in the cytoplasm of cancer cells. Hsp70 thus serves as a convenient, non-discriminating transporter of antigens and can protect the peptides during internalization by APC and cross presentation to T lymphocytes. We describe a method for purifying Hsp70-peptide complexes that can be used to prepare molecular chaperonebased vaccines, involving sequential gel fi ltration, ion exchange, and af fi nity chromatography. © Springer Science+Business Media, LLC 2013.