{"id":{"repo_id":"cornell","oai_identifier":"oai:ecommons.cornell.edu:1813/67663"},"canonical_url":"https://search.dev.ndltd.org/etd/cornell/oai:ecommons.cornell.edu:1813/67663","repository":{"repo_id":"cornell","name":"Cornell University","base_url":"https://ecommons.cornell.edu/server/oai/request"},"display":{"title":"Engineered Oligosaccharyltransferases With Unique N-Glycosylation Site Preferences","abstract":"The key enzyme in the Campylobacter jejuni glycosylation pathway, PglB, has been one of the well-studied asparagine-linked oligosaccharyltransferase (OST) in bacterial glycoengineering area. While C. jejuni PglB performs well in transferring different glycans, the acceptor sites it can recognize are limited. We provided a thorough investigation into Desulfovibrio desulfuricans PglB (DdPglB), an OST sharing homology with C. jejuni PglB but having more relaxed sequon specificity. The sequon logo of DdPglB against XXNXT library were built through a high-throughput assay. Two engineered OSTs combining distinct transmembrane domain and periplasmic domain of PglBs from C. jejuni and D. desulfuricans was also investigated. And the study interestingly revealed they can lose all their glycosylation activities after the combination. According to the sequon logo we built and further verification, a notable sequon QYNST, which is a native acceptor sequon of Fc domain of human immunoglobulin G, was able to be glycosylated by DdPglB. Overall, we presented a series of sequons that can be glycosylated by DdPglB and further expanded the glycoengineering toolbox with more potential acceptor sites that were not glycosylated before.","abstract_html":"The key enzyme in the Campylobacter jejuni glycosylation pathway, PglB, has been one of the well-studied asparagine-linked oligosaccharyltransferase (OST) in bacterial glycoengineering area. While C. jejuni PglB performs well in transferring different glycans, the acceptor sites it can recognize are limited. We provided a thorough investigation into Desulfovibrio desulfuricans PglB (DdPglB), an OST sharing homology with C. jejuni PglB but having more relaxed sequon specificity. The sequon logo of DdPglB against XXNXT library were built through a high-throughput assay. Two engineered OSTs combining distinct transmembrane domain and periplasmic domain of PglBs from C. jejuni and D. desulfuricans was also investigated. And the study interestingly revealed they can lose all their glycosylation activities after the combination. According to the sequon logo we built and further verification, a notable sequon QYNST, which is a native acceptor sequon of Fc domain of human immunoglobulin G, was able to be glycosylated by DdPglB. Overall, we presented a series of sequons that can be glycosylated by DdPglB and further expanded the glycoengineering toolbox with more potential acceptor sites that were not glycosylated before.","abstract_has_math":false,"creators":["Chen, Feng-Yang"],"institution":"Cornell University","degree_name":"M.S., Chemical Engineering","degree_level":"Master of Science","degree_discipline":"Chemical Engineering","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":["Daniel, Susan","Paszek, Matthew J."],"year":2019,"date_issued":"2019-08-30","date_published":"2019-08-30","updated_at":"2026-07-24T01:49:06Z","subjects":["Chemical engineering","Campylobacter jejuni","Desulfovibrio desulfuricans","Glycosylation","Oligosaccharyltransferases","PglB","sequon logo","Biomedical engineering"],"languages":["en_US"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier.doi","label":"DOI","values":["https://doi.org/10.7298/s792-kt31"],"render_values":[{"text":"https://doi.org/10.7298/s792-kt31","href":"https://doi.org/10.7298/s792-kt31","code":true}]},{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["ProQuest Submission ID: 10624","ProQuest Publication ID: 13904844"],"render_values":[{"text":"ProQuest Submission ID: 10624","href":null,"code":true},{"text":"ProQuest Publication ID: 13904844","href":null,"code":true}]}]},"links":{"outbound_url":"https://hdl.handle.net/1813/67663","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Daniel, Susan","Paszek, Matthew J."]},{"key":"dc:creator","label":"Author","values":["Chen, Feng-Yang"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2019-10-15T16:49:27Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2019-10-15T16:49:27Z"]},{"key":"dc:date.issued","label":"Date","values":["2019-08-30"]},{"key":"dc:type","label":"Dc Type","values":["dissertation or thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemical Engineering"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Master of Science"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M.S., Chemical Engineering"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Cornell University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemical engineering","Campylobacter jejuni","Desulfovibrio desulfuricans","Glycosylation","Oligosaccharyltransferases","PglB","sequon logo","Biomedical engineering"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en_US"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.doi","label":"DOI","values":["https://doi.org/10.7298/s792-kt31"]},{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["ProQuest Submission ID: 10624","ProQuest Publication ID: 13904844"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/1813/67663"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The key enzyme in the Campylobacter jejuni glycosylation pathway, PglB, has been one of the well-studied asparagine-linked oligosaccharyltransferase (OST) in bacterial glycoengineering area. While C. jejuni PglB performs well in transferring different glycans, the acceptor sites it can recognize are limited. We provided a thorough investigation into Desulfovibrio desulfuricans PglB (DdPglB), an OST sharing homology with C. jejuni PglB but having more relaxed sequon specificity. The sequon logo of DdPglB against XXNXT library were built through a high-throughput assay. Two engineered OSTs combining distinct transmembrane domain and periplasmic domain of PglBs from C. jejuni and D. desulfuricans was also investigated. And the study interestingly revealed they can lose all their glycosylation activities after the combination. According to the sequon logo we built and further verification, a notable sequon QYNST, which is a native acceptor sequon of Fc domain of human immunoglobulin G, was able to be glycosylated by DdPglB. Overall, we presented a series of sequons that can be glycosylated by DdPglB and further expanded the glycoengineering toolbox with more potential acceptor sites that were not glycosylated before."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Engineered Oligosaccharyltransferases With Unique N-Glycosylation Site Preferences"]}]}],"canonical_facts":{"dc:contributor.committeemember":["Daniel, Susan","Paszek, Matthew J."],"dc:creator":["Chen, Feng-Yang"],"dc:date.accessioned":["2019-10-15T16:49:27Z"],"dc:date.available":["2019-10-15T16:49:27Z"],"dc:date.issued":["2019-08-30"],"dc:description.abstract":["The key enzyme in the Campylobacter jejuni glycosylation pathway, PglB, has been one of the well-studied asparagine-linked oligosaccharyltransferase (OST) in bacterial glycoengineering area. While C. jejuni PglB performs well in transferring different glycans, the acceptor sites it can recognize are limited. We provided a thorough investigation into Desulfovibrio desulfuricans PglB (DdPglB), an OST sharing homology with C. jejuni PglB but having more relaxed sequon specificity. The sequon logo of DdPglB against XXNXT library were built through a high-throughput assay. Two engineered OSTs combining distinct transmembrane domain and periplasmic domain of PglBs from C. jejuni and D. desulfuricans was also investigated. And the study interestingly revealed they can lose all their glycosylation activities after the combination. According to the sequon logo we built and further verification, a notable sequon QYNST, which is a native acceptor sequon of Fc domain of human immunoglobulin G, was able to be glycosylated by DdPglB. Overall, we presented a series of sequons that can be glycosylated by DdPglB and further expanded the glycoengineering toolbox with more potential acceptor sites that were not glycosylated before."],"dc:format.mimetype":["application/pdf"],"dc:identifier.doi":["https://doi.org/10.7298/s792-kt31"],"dc:identifier.other":["ProQuest Submission ID: 10624","ProQuest Publication ID: 13904844"],"dc:identifier.uri":["https://hdl.handle.net/1813/67663"],"dc:language.iso":["en_US"],"dc:subject":["Chemical engineering","Campylobacter jejuni","Desulfovibrio desulfuricans","Glycosylation","Oligosaccharyltransferases","PglB","sequon logo","Biomedical engineering"],"dc:title":["Engineered Oligosaccharyltransferases With Unique N-Glycosylation Site Preferences"],"dc:type":["dissertation or thesis"],"thesis:degree_discipline":["Chemical Engineering"],"thesis:degree_level":["Master of Science"],"thesis:degree_name":["M.S., Chemical Engineering"],"thesis:institution_name":["Cornell University"]},"updated_at":"2026-07-24T01:49:06Z"}