The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells.

Abstract:

:The chaperone glucose-regulated protein 94 (GRP94) has long been used to augment peptide presentation to T cells. This chaperone binds antigenic peptides, binds to receptors on professional antigen-presenting cells (APCs), activates these cells and after internalization, transfers the peptides to MHC class I for activation of T cells. Here we show that all these activities reside within amino acids 1-355 of GRP94. This small fragment is sufficient to bind peptides, to bind and be taken up by the receptors CD91 and scavenger receptor type A on either dendritic cells or macrophages. The minimal construct can augment peptide presentation in culture and induce antigen-specific CTL in naive mice only because it loads APCs with the relevant peptide. Thus, the sequence 1-355 is the immunologically sufficient module of GRP94 and we propose that this 'mini-chaperone' can be used in immunotherapy of tumors and vaccine development.

journal_name

Int Immunol

journal_title

International immunology

authors

Biswas C,Sriram U,Ciric B,Ostrovsky O,Gallucci S,Argon Y

doi

10.1093/intimm/dxl049

subject

Has Abstract

pub_date

2006-07-01 00:00:00

pages

1147-57

issue

7

eissn

0953-8178

issn

1460-2377

pii

dxl049

journal_volume

18

pub_type

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