{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/117887"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/117887","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Investigating the molecular mechanisms of chaperones involved in antigen presentation","abstract":"Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2024-08-01","abstract_html":"Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2024-08-01","abstract_has_math":false,"creators":["Devlin, Christine Anne"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Procko, Erik","Kranz, David","Stadtmueller, Beth","Nair, Satish"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2022,"date_issued":"2022-08","date_published":"2022-08","updated_at":"2026-07-22T22:24:56Z","subjects":["immunology","protein"],"languages":["en","eng"],"rights":["Copyright 2022 Christine Devlin"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/2142/117887","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Procko, Erik","Kranz, David","Stadtmueller, Beth","Nair, Satish"]},{"key":"dc:creator","label":"Author","values":["Devlin, Christine Anne"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2022-08","2022-06-14"]},{"key":"dc:type","label":"Dc Type","values":["text","Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["immunology","protein"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en","eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 2022 Christine Devlin"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://hdl.handle.net/2142/117887"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2024-08-01","The student, Christine Devlin, accepted the attached license on 2022-06-08 at 22:47.","The student, Christine Devlin, submitted this Dissertation for approval on 2022-06-08 at 22:57.","This Dissertation was approved for publication on 2022-06-14 at 13:51.","DSpace SAF Submission Ingestion Package generated from Vireo submission #18064 on 2023-05-11 at 17:07:36","Class I major histocompatibility complexes (MHC-I) play an important role in the adaptive immune system as they present peptides on the cell surface. Peptides from non-self proteins can be recognized by surveilling T cells leading to cell lysis. The mechanism of peptide loading, termed antigen presentation, by chaperones, tapasin and TAPBPR, is unclear. Here, using biochemical and biophysical assays, I characterize the mechanism of TAPBPR, a chaperone and peptide editor that is independent of the peptide loading complex. First, I show that TAPBPR can bind as a chaperone with broad MHC-I allelic recognition but has narrow MHC-I specificity in regard to peptide editing. Additionally, there is a folded protein motif within the α2 helix of the MHC-I that TAPBPR is recognizing to bind as a chaperone. Second, I show that the proposed “scoop loop” of TAPBPR is unimportant for chaperoning ability and show that the important regions of TAPBPR for this activity are located where the protein interacts with the base of the MHC-I α2 helix as Ill as beta-2-microglobulin. Third, I engineered a version of TAPBPR with dual functions of chaperone and peptide editor of multiple HLA-A alleles. Overall, this work provides further insight into the mechanisms involved in antigen presentation."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Investigating the molecular mechanisms of chaperones involved in antigen presentation"]}]}],"canonical_facts":{"dc:contributor":["Procko, Erik","Kranz, David","Stadtmueller, Beth","Nair, Satish"],"dc:creator":["Devlin, Christine Anne"],"dc:date":["2022-08","2022-06-14"],"dc:description":["Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2024-08-01","The student, Christine Devlin, accepted the attached license on 2022-06-08 at 22:47.","The student, Christine Devlin, submitted this Dissertation for approval on 2022-06-08 at 22:57.","This Dissertation was approved for publication on 2022-06-14 at 13:51.","DSpace SAF Submission Ingestion Package generated from Vireo submission #18064 on 2023-05-11 at 17:07:36","Class I major histocompatibility complexes (MHC-I) play an important role in the adaptive immune system as they present peptides on the cell surface. Peptides from non-self proteins can be recognized by surveilling T cells leading to cell lysis. The mechanism of peptide loading, termed antigen presentation, by chaperones, tapasin and TAPBPR, is unclear. Here, using biochemical and biophysical assays, I characterize the mechanism of TAPBPR, a chaperone and peptide editor that is independent of the peptide loading complex. First, I show that TAPBPR can bind as a chaperone with broad MHC-I allelic recognition but has narrow MHC-I specificity in regard to peptide editing. Additionally, there is a folded protein motif within the α2 helix of the MHC-I that TAPBPR is recognizing to bind as a chaperone. Second, I show that the proposed “scoop loop” of TAPBPR is unimportant for chaperoning ability and show that the important regions of TAPBPR for this activity are located where the protein interacts with the base of the MHC-I α2 helix as Ill as beta-2-microglobulin. Third, I engineered a version of TAPBPR with dual functions of chaperone and peptide editor of multiple HLA-A alleles. Overall, this work provides further insight into the mechanisms involved in antigen presentation."],"dc:format":["application/pdf"],"dc:identifier":["https://hdl.handle.net/2142/117887"],"dc:language":["en","eng"],"dc:rights":["Copyright 2022 Christine Devlin"],"dc:subject":["immunology","protein"],"dc:title":["Investigating the molecular mechanisms of chaperones involved in antigen presentation"],"dc:type":["text","Thesis"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:24:56Z"}