UPMC Hillman Cancer Center

Robert J. Binder, PhD

Robert Binder
Associate Professor of Immunology


Contact Information

Contact Information

E1051 BSTWR
200 Lothrop St.
Pittsburgh, PA 15261

Email: rjb42@pitt.edu

Research Keywords

Research Keywords

Antigen cross-presentation; tumor immunology; immunotherapy; heat shock proteins; cancer vaccines

Research Summary

Research Summary


A mechanism for antigen transfer, cross-presentation and priming of T cell responses. Oncoimmunology 3, e28222.

Our research interests are focused on the mechanisms of cross-priming of antigens during immune responses to cancer, viruses and autoimmunity. The pursuit of this research area stems from the observations that in many situations, heat shock proteins (HSPs) are both necessary and sufficient for cross-presentation. HSPs are adept at this because of several unique properties, including their ability to:

  1. chaperone peptides;
  2. bind to HSP receptors (CD91) for endocytosis; and
  3. stimulate immune cells to up-regulate costimulation.

HSPs thus elicit remarkable immune responses specific for the peptides they chaperone. The laboratory is using these observations to examine new facets of antigen presentation and also to develop novel immunotherapies for cancer, infectious disease and autoimmune disorders.

A related area of research examines how other ligands for the HSP receptor CD91 interact with the immune system. In the past few years, we have shown that a2-macroglobulin (a2M), a CD91 ligand, though not a bonafide HSP, shares the immunogenic properties of HSPs and can elicit immune responses specific to (peptide) substrates that it chaperones. We are currently exploring the identification of naturally formed a2M-substrate complexes and the potential use of these immunogenic complexes as therapeutic agents for cancer and infectious disease.

Selected Publications

Selected Publications

  • Zhou, YJ, Messmer MN, Binder RJ. Establishment of tumor-associated immunity requires interaction of heat shock proteins with CD91. Cancer Immunol Res. 2014 Mar;2(3):217-28. PubMed Link
  • Messmer MN, Pasmowitz J, Kropp LE, Watkins SC, Binder RJ. Identification of the cellular sentinels for native immunogenic heat shock proteins in vivo. J Immunol. 2013 Oct 15;191(8):4456-65. PubMed Link
  • Pawaria S and Binder RJ. CD91-dependent programming of T helper cell responses following heat shock protein immunization. Nat Commun. 2011 Nov 1;2:521. PubMed Link
  • Kropp LE, Garg M, Binder RJ. Ovalbumin-derived precursor peptides are transferred sequentially from gp96 and calreticulin to MHC I in the endoplasmic reticulum. J Immunol. 2010 May 15;184(10):5619-27. PubMed Link
  • Binder RJ and Srivastava PK. Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8+ T cells. Nat Immunol. 2005 Jun;6(6):593-9. PubMed Link
  • Binder RJ and Srivastava PK. Essential role of CD91 in re-presentation of gp96-chaperoned peptides. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6128-33. PubMed Link
  • Basu S, Binder RJ, Ramalingham T, Srivastava PK. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70 and calreticulin. Immunity. 2001 Mar;14(3):303-13. PubMed Link
  • Binder RJ, Blachere NE, Srivastava PK. Heat shock protein-chaperoned peptides but not free peptides introduced into the cytosol are presented efficiently by MHC I molecules. J Biol Chem. 2001 May 18;276(20):17163-71. PubMed Link

See all pubs (Pubmed)

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Last modified: 6/27/14