An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response.

Zihai Li, Jie Dai, Hong Zheng, Bei Liu, Marissa Caudill

Research output: Contribution to journalReview article

48 Citations (Scopus)

Abstract

Heat shock protein (HSP) gp96, or grp94 is an endoplasmic reticular (ER) paralog of the cytosolic HSP90. Being abundant and non-polymorphic, gp96 plays significant roles in maintaining protein homeostasis in the secretory pathway. This "house-keeping" role of gp96 has now been overshadowed by the intriguing findings that gp96 modulates both the innate and adaptive components of the immune system. It has been found that, (i) gp96 is one of the major peptide binding proteins in the ER, (ii) gp96 interacts specifically with receptors including CD91 and possibly toll-like receptors (TLRs), on the surface of professional antigen presenting cells (APCs), (iii) interaction with APCs leads to re-presentation of gp96-chaperoned peptides to the major histocompatibility complex (MHC) molecules of APCs, (iv) direct access of gp96 to APCs triggers functional activation of APCs. In this review, we will examine each of these immunological attributes of gp96 critically. As experimentalists, we will also propose specific experiments to examine the argument that gp96, perhaps along with other members of HSP family, is the antigenic carrier for mediating cross priming of antigen-specific T lymphocytes in vertebrates.

Original languageEnglish (US)
JournalFrontiers in bioscience : a journal and virtual library
Volume7
DOIs
StatePublished - Jan 1 2002

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Antigen-Presenting Cells
Heat-Shock Proteins
Peptides
Cross-Priming
T-cells
Immune system
Toll-Like Receptors
Secretory Pathway
Surface Antigens
Major Histocompatibility Complex
Cell Communication
Vertebrates
Immune System
Carrier Proteins
Homeostasis
Chemical activation
T-Lymphocytes
Antigens
Molecules
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

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abstract = "Heat shock protein (HSP) gp96, or grp94 is an endoplasmic reticular (ER) paralog of the cytosolic HSP90. Being abundant and non-polymorphic, gp96 plays significant roles in maintaining protein homeostasis in the secretory pathway. This {"}house-keeping{"} role of gp96 has now been overshadowed by the intriguing findings that gp96 modulates both the innate and adaptive components of the immune system. It has been found that, (i) gp96 is one of the major peptide binding proteins in the ER, (ii) gp96 interacts specifically with receptors including CD91 and possibly toll-like receptors (TLRs), on the surface of professional antigen presenting cells (APCs), (iii) interaction with APCs leads to re-presentation of gp96-chaperoned peptides to the major histocompatibility complex (MHC) molecules of APCs, (iv) direct access of gp96 to APCs triggers functional activation of APCs. In this review, we will examine each of these immunological attributes of gp96 critically. As experimentalists, we will also propose specific experiments to examine the argument that gp96, perhaps along with other members of HSP family, is the antigenic carrier for mediating cross priming of antigen-specific T lymphocytes in vertebrates.",
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An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response. / Li, Zihai; Dai, Jie; Zheng, Hong; Liu, Bei; Caudill, Marissa.

In: Frontiers in bioscience : a journal and virtual library, Vol. 7, 01.01.2002.

Research output: Contribution to journalReview article

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