Antigen Delivery Controlled by an On‐Demand Photorelease
Abstract: To eliminate infected and cancerous cells, antigen processing and presentation play a pivotal role through the recognition of antigenic peptides displayed on Major Histocompatibility Complex class I (MHC I) molecules. Here, we developed a photostimulated antigen release system that enables the temporal inception of antigen flux. Simple and effective photocaging of the human immunodeficiency virus (HIV)‐Nef73‐derived epitope, a representative high‐affinity MHC I ligand, was provided by steric hindrance to block the recognition by the transporter associated with antigen processing (TAP) in the peptide loading complex (PLC). In response to light, a heteronomous release of antigens and subsequent translocation in various scenarios is demonstrated, including a TAP‐related ATP‐binding cassette (ABC) transporter reconstituted in liposomes and the native PLC in the endoplasmic reticulum (ER) membrane of human cells. The photochemically induced ‘burst’ of antigens opens new opportunities for a mechanistic analysis of the antigen translocation machinery and will help to provide insights into antigen processing pathways via an on‐demand, subcellular pulse‐chase release of antigens.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Antigen Delivery Controlled by an On‐Demand Photorelease ; day:12 ; month:07 ; year:2024 ; extent:8
Angewandte Chemie ; (12.07.2024) (gesamt 8)
- Creator
- DOI
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10.1002/ange.202405035
- URN
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urn:nbn:de:101:1-2407121448319.148628077370
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:50 AM CEST
Data provider
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Löffler, Max
- Frühschulz, Stefan
- Rockel, Zoe
- Pečak, Matija
- Tampé, Robert
- Wieneke, Ralph
Other Objects (12)
Antigen Delivery Controlled by an On‐Demand Photorelease
Zur Wechselwirkung von Glycophorin mit Lipidkomponenten in künstlichen Phospholipid-Doppelschichten : eine spektroskopische, elektronenmikroskopische und kalorimetrische Studie zur Lipid-Protein-Wechselwirkung
Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
Mechanistic and structural insights into the quality control of the MHC I antigen processing pathway
Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex
Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)
Structural and functional analysis of the MHC I–tapasin–ERp57 multi-chaperone complex in antigen processing and presentation
Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **
Zeitaufgelöste Mn 2+ −NO‐ und NO−NO‐Abstandsmessungen zeigen regulierende Funktion der katalytischen Asymmetrie auf den alternierenden Zugang in einem ABC‐Transporter **
Proofreading of peptide—MHC complexes through dynamic multivalent interactions
An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP (transporter associated with antigen processing)
Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)
Antigen Delivery Controlled by an On‐Demand Photorelease
Zur Wechselwirkung von Glycophorin mit Lipidkomponenten in künstlichen Phospholipid-Doppelschichten : eine spektroskopische, elektronenmikroskopische und kalorimetrische Studie zur Lipid-Protein-Wechselwirkung
Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
Mechanistic and structural insights into the quality control of the MHC I antigen processing pathway
Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex
Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)
Structural and functional analysis of the MHC I–tapasin–ERp57 multi-chaperone complex in antigen processing and presentation
Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **
Zeitaufgelöste Mn 2+ −NO‐ und NO−NO‐Abstandsmessungen zeigen regulierende Funktion der katalytischen Asymmetrie auf den alternierenden Zugang in einem ABC‐Transporter **
Proofreading of peptide—MHC complexes through dynamic multivalent interactions
An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP (transporter associated with antigen processing)
Selective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)
Antigen Delivery Controlled by an On‐Demand Photorelease
Zur Wechselwirkung von Glycophorin mit Lipidkomponenten in künstlichen Phospholipid-Doppelschichten : eine spektroskopische, elektronenmikroskopische und kalorimetrische Studie zur Lipid-Protein-Wechselwirkung
Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
Mechanistic and structural insights into the quality control of the MHC I antigen processing pathway
Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex
Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)
Structural and functional analysis of the MHC I–tapasin–ERp57 multi-chaperone complex in antigen processing and presentation
Time‐Resolved Mn 2+ −NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter **
Zeitaufgelöste Mn 2+ −NO‐ und NO−NO‐Abstandsmessungen zeigen regulierende Funktion der katalytischen Asymmetrie auf den alternierenden Zugang in einem ABC‐Transporter **
Proofreading of peptide—MHC complexes through dynamic multivalent interactions
An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP (transporter associated with antigen processing)