Robert Binder

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Complexes of the heat shock protein gp96 and antigenic peptides are taken up by antigen-presenting cells and presented by MHC class I molecules. In order to explain the unusual efficiency of this process, the uptake of gp96 had been postulated to occur through a receptor, identified recently as CD91. We show here that complexes of peptides with heat shock(More)
Dendritic cells (DC) are key components of innate and adaptive immune responses. The identity of endogenous signals that activate DC is a crucial and unresolved question. We report here that heat shock proteins (HSP), the most abundant and conserved mammalian molecules, constitute such an internal signal. Necrotic but not apoptotic cell death leads to(More)
Antigen presenting cells (APCs) can take up exogenous antigenic peptides chaperoned by heat shock protein gp96 and re-present them through the endogenous pathway on their major histocompatibility class I molecules. The high efficiency of this process has been attributed previously to a receptor for gp96 on APCs. The CD91 molecule (also called(More)
The existence of heat-shock protein (HSP) receptors on antigen-presenting cells (APCs) was hypothesized in 1994. The first such receptor, CD91 or LRP, was identified and characterized in 2000. The pace of attribution has quickened since and during the last three years alone, six putative HSP receptors have been identified. These include CD40, LOX-1, CD36,(More)
The studies reported here bear on the events in the cytosol that lead to trafficking of peptides during antigen processing and presentation by major histocompatibility complex (MHC) I molecules. We have introduced free antigenic peptides or antigenic peptides bound to serum albumin or to cytosolic heat shock proteins hsp90 (and its endoplasmic reticular(More)
The form in which antigens are transferred from cancer cells or infected cells to antigen-presenting cells as a part of the process of priming CD8+ T cells has been a longstanding unresolved issue. Intact proteins or protein fragments in the form of free peptides or peptides chaperoned by heat-shock protein are possible sources of antigen. We address this(More)
Heat shock proteins (HSPs) such as gp96 are released from cells as a result of necrotic cell death. The ability of endogenous HSP-peptide complexes to elicit antigen-specific T cells requires representation of the chaperoned peptides by antigen-presenting cells. Re-presentation requires the uptake of HSP-peptide complexes through a receptor, suggested to be(More)
We recently have identified CD91 as a receptor for the heat shock protein gp96. CD91 was identified initially as a receptor for alpha(2)-macroglobulin (alpha(2)M). Gp96 and alpha(2)M are both ligands for CD91. Because gp96-chaperoned peptides can prime CD8(+) T cell responses and are re-presented by APCs, we tested alpha(2)M for similar properties. Our(More)
Almost 60 years ago, the pioneering work of George Klein and others showed that cancers could be made targets for the immune system. Identification of the tumor targets, known as tumor antigens, became a focus in cancer biology that led to the discovery of the immunological properties of heat-shock proteins (HSPs) in 1986 by Pramod Srivastava and(More)