{"id":{"repo_id":"cambridge","oai_identifier":"oai:www.repository.cam.ac.uk:1810/374983"},"canonical_url":"https://search.dev.ndltd.org/etd/cambridge/oai:www.repository.cam.ac.uk:1810/374983","repository":{"repo_id":"cambridge","name":"Cambridge University","base_url":"https://api.repository.cam.ac.uk/server/oai/request"},"display":{"title":"N-Glycosylation Protects Host from Mycobacterial Infection","abstract":"Host immunity against tuberculosis (TB) is primarily mediated by macrophages. Macrophages phagocytose *Mycobacterium tuberculosis* and restrict their growth. Through a zebrafish forward genetic screen, we have identified the early steps of N-glycosylation are required for the macrophage to resist mycobacterial infections. N-glycosylation attaches an oligosaccharide molecule to nascent secretory or membrane proteins within the endoplasmic reticulum (ER) for protein folding and trafficking. Defects of N-glycosylation induce the unfolded protein response (UPR), which sensitizes infected macrophages to intrinsic apoptosis. This apoptosis differs from the cell death observed in infected wild-type cells and is not dependent on mycobacterial virulence factors. Therefore, N-glycosylation provides protection by mitigating the ER stress of protein synthesis triggered by cellular responses to mycobacterial infection.","abstract_html":"Host immunity against tuberculosis (TB) is primarily mediated by macrophages. Macrophages phagocytose *Mycobacterium tuberculosis* and restrict their growth. Through a zebrafish forward genetic screen, we have identified the early steps of N-glycosylation are required for the macrophage to resist mycobacterial infections. N-glycosylation attaches an oligosaccharide molecule to nascent secretory or membrane proteins within the endoplasmic reticulum (ER) for protein folding and trafficking. Defects of N-glycosylation induce the unfolded protein response (UPR), which sensitizes infected macrophages to intrinsic apoptosis. This apoptosis differs from the cell death observed in infected wild-type cells and is not dependent on mycobacterial virulence factors. Therefore, N-glycosylation provides protection by mitigating the ER stress of protein synthesis triggered by cellular responses to mycobacterial infection.","abstract_has_math":false,"creators":["Lyu, Bingnan"],"institution":"University of Cambridge","degree_name":"Doctor of Philosophy (PhD)","degree_level":"Doctoral","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Ramakrishnan, Lalita"],"committee_chairs":[],"committee_members":[],"year":2024,"date_issued":"2024-03-29","date_published":"2024-03-29","updated_at":"2026-07-22T22:24:04Z","subjects":["Cell Death","ER Stress","Macrophage","N-glycosylation","Tuberculosis"],"languages":["eng"],"rights":[],"rights_urls":["https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/896d9b2b-7444-4eb4-affe-1b9416992367/download","https://www.rioxx.net/licenses/all-rights-reserved/"],"identifier_entries":[]},"links":{"outbound_url":"https://doi.org/10.17863/CAM.112837","outbound_label":"DOI","outbound_source":"dc:identifier.doi"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Ramakrishnan, Lalita"]},{"key":"dc:creator","label":"Author","values":["Lyu, Bingnan"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.issued","label":"Date","values":["2024-03-29"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["University of Cambridge"]},{"key":"dc:relation.isreferencedby.uri","label":"Dc Relation Isreferencedby URI","values":["https://www.repository.cam.ac.uk/handle/1810/374983"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["Doctoral"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Cell Death","ER Stress","Macrophage","N-glycosylation","Tuberculosis"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/896d9b2b-7444-4eb4-affe-1b9416992367/download","https://www.rioxx.net/licenses/all-rights-reserved/"]},{"key":"dc:rights.embargodate","label":"Dc Rights Embargodate","values":["2025-10-18"]},{"key":"dc:rights.embargotype","label":"Dc Rights Embargotype","values":["embargo"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.doi","label":"DOI","values":["https://doi.org/10.17863/CAM.112837"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://apollo8-f-pro.lib.cam.ac.uk/bitstreams/e7eb227e-6466-47d8-b96b-84d8af5741be/download"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Host immunity against tuberculosis (TB) is primarily mediated by macrophages. 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