Work

Purification, Preparation, and Use of Chaperone–Peptide Complexes for Tumor Immunotherapy

Year: 2012

Type: book-chapter

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 chaperone-based vaccines, involving sequential gel filtration, ion exchange, and affinity chromatography.

Source: Methods in molecular biology

DOI: 10.1007/978-1-62703-218-6_17

Authors: Ayesha Murshid, Jianlin Gong, Stuart K. Calderwood

Institutions: Beth Israel Deaconess Medical Center, Harvard University, Boston University

Language: English

Topic: Heat shock proteins research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green