2026-09-20T03:11:07Zhttps://ecommons.cornell.edu/server/oai/requestoai:ecommons.cornell.edu:1813/676632026-05-15T19:42:00Zcom_1813_35col_1813_47
Chen, Feng-Yang
Delisa, Matthew
Daniel, Susan
Paszek, Matthew J.
2019-10-15T16:49:27Z
2019-10-15T16:49:27Z
2019-08-30
ProQuest Submission ID: 10624
ProQuest Publication ID: 13904844
https://hdl.handle.net/1813/67663
https://doi.org/10.7298/s792-kt31
11050647
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.
en_US
Chemical engineering
Campylobacter jejuni
Desulfovibrio desulfuricans
Glycosylation
Oligosaccharyltransferases
PglB
sequon logo
Biomedical engineering
Engineered Oligosaccharyltransferases With Unique N-Glycosylation Site Preferences
dissertation or thesis
application/pdf
Chemical Engineering
Cornell University
Master of Science
M.S., Chemical Engineering
https://hdl.handle.net/1813/59810
Publication
Cornell Theses and Dissertations
Chen, Feng-Yang
5893a6ea-7af3-41d7-abc6-04bcd26ab5df
open.access
open.access
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<Title>Engineered Oligosaccharyltransferases With Unique N-Glycosylation Site Preferences</Title>
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<DOI>https://doi.org/10.7298/s792-kt31</DOI>
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<Keyword>Chemical engineering</Keyword>
<Keyword>Campylobacter jejuni</Keyword>
<Keyword>Desulfovibrio desulfuricans</Keyword>
<Keyword>Glycosylation</Keyword>
<Keyword>Oligosaccharyltransferases</Keyword>
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<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>
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