The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells
Identifieur interne : 002D62 ( Main/Exploration ); précédent : 002D61; suivant : 002D63The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells
Auteurs : Chhanda Biswas [États-Unis] ; Uma Sriram [États-Unis] ; Bogoljub Ciric [États-Unis] ; Olga Ostrovsky [États-Unis] ; Stefania Gallucci [États-Unis] ; Yair Argon [États-Unis]Source :
- International Immunology [ 0953-8178 ] ; 2006.
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.
Url:
DOI: 10.1093/intimm/dxl049
Affiliations:
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19104</wicri:noRegion></affiliation></author><author><name sortKey="Ciric, Bogoljub" sort="Ciric, Bogoljub" uniqKey="Ciric B" first="Bogoljub" last="Ciric">Bogoljub Ciric</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology and Laboratory Medicine, Children's Hospital of Philadelphia and University of Pennsylvania, Philadelphia, PA 19104</wicri:regionArea><wicri:noRegion>PA 19104</wicri:noRegion></affiliation></author><author><name sortKey="Ostrovsky, Olga" sort="Ostrovsky, Olga" uniqKey="Ostrovsky O" first="Olga" last="Ostrovsky">Olga Ostrovsky</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology and Laboratory Medicine, Children's Hospital of Philadelphia and University of Pennsylvania, Philadelphia, PA 19104</wicri:regionArea><wicri:noRegion>PA 19104</wicri:noRegion></affiliation></author><author><name sortKey="Gallucci, Stefania" sort="Gallucci, Stefania" uniqKey="Gallucci S" first="Stefania" last="Gallucci">Stefania Gallucci</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pediatrics, Children's Hospital of Philadelphia and University of Pennsylvania, Philadelphia, PA 19104</wicri:regionArea><wicri:noRegion>PA 19104</wicri:noRegion></affiliation></author><author><name sortKey="Argon, Yair" sort="Argon, Yair" uniqKey="Argon Y" first="Yair" last="Argon">Yair Argon</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology and Laboratory Medicine, Children's Hospital of Philadelphia and University of Pennsylvania, Philadelphia, PA 19104</wicri:regionArea><wicri:noRegion>PA 19104</wicri:noRegion></affiliation><affiliation wicri:level="1"><country wicri:rule="url">États-Unis</country></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">International Immunology</title><idno type="eISSN">1460-2377</idno><idno type="ISSN">0953-8178</idno><imprint><publisher>Oxford University Press</publisher><date>2006</date><date type="e-published">2006</date><biblScope unit="vol">18</biblScope><biblScope unit="issue">7</biblScope><biblScope unit="page" from="1147">1147</biblScope><biblScope unit="page" to="1157">1157</biblScope></imprint><idno type="ISSN">0953-8178</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0953-8178</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="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.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Biswas, Chhanda" sort="Biswas, Chhanda" uniqKey="Biswas C" first="Chhanda" last="Biswas">Chhanda Biswas</name></noRegion><name sortKey="Argon, Yair" sort="Argon, Yair" uniqKey="Argon Y" first="Yair" last="Argon">Yair Argon</name><name sortKey="Argon, Yair" sort="Argon, Yair" uniqKey="Argon Y" first="Yair" last="Argon">Yair Argon</name><name sortKey="Ciric, Bogoljub" sort="Ciric, Bogoljub" uniqKey="Ciric B" first="Bogoljub" last="Ciric">Bogoljub Ciric</name><name sortKey="Gallucci, Stefania" sort="Gallucci, Stefania" uniqKey="Gallucci S" first="Stefania" last="Gallucci">Stefania Gallucci</name><name sortKey="Ostrovsky, Olga" sort="Ostrovsky, Olga" uniqKey="Ostrovsky O" first="Olga" last="Ostrovsky">Olga Ostrovsky</name><name sortKey="Sriram, Uma" sort="Sriram, Uma" uniqKey="Sriram U" first="Uma" last="Sriram">Uma Sriram</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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