Display of the human mucinome with defined O-glycans by gene engineered cells
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , , , , , , , , , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | https://hdl.handle.net/10216/150450 |
Resumo: | Mucins are a large family of heavily O-glycosylated proteins that cover all mucosal surfaces and constitute the major macromolecules in most body fluids. Mucins are primarily defined by their variable tandem repeat (TR) domains that are densely decorated with different O-glycan structures in distinct patterns, and these arguably convey much of the informational content of mucins. Here, we develop a cell-based platform for the display and production of human TR O-glycodomains (~200 amino acids) with tunable structures and patterns of O-glycans using membrane-bound and secreted reporters expressed in glycoengineered HEK293 cells. Availability of defined mucin TR O-glycodomains advances experimental studies into the versatile role of mucins at the interface with pathogenic microorganisms and the microbiome, and sparks new strategies for molecular dissection of specific roles of adhesins, glycoside hydrolases, glycopeptidases, viruses and other interactions with mucin TRs as highlighted by examples. |
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Display of the human mucinome with defined O-glycans by gene engineered cellsMucins are a large family of heavily O-glycosylated proteins that cover all mucosal surfaces and constitute the major macromolecules in most body fluids. Mucins are primarily defined by their variable tandem repeat (TR) domains that are densely decorated with different O-glycan structures in distinct patterns, and these arguably convey much of the informational content of mucins. Here, we develop a cell-based platform for the display and production of human TR O-glycodomains (~200 amino acids) with tunable structures and patterns of O-glycans using membrane-bound and secreted reporters expressed in glycoengineered HEK293 cells. Availability of defined mucin TR O-glycodomains advances experimental studies into the versatile role of mucins at the interface with pathogenic microorganisms and the microbiome, and sparks new strategies for molecular dissection of specific roles of adhesins, glycoside hydrolases, glycopeptidases, viruses and other interactions with mucin TRs as highlighted by examples.Nature Pub. Group20212021-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10216/150450eng2041-172310.1038/s41467-021-24366-4Nason, RBüll, CKonstantinidi, ASun, LYe, ZHalim, ADu, WSørensen, DMDurbesson, FFurukawa, SMandel, UJoshi, HJDworkin, LAHansen, LDavid, LIverson, TMBensing, BASullam, PMVarki, AVries, EHaan, CAMVincentelli, RHenrissat, BVakhrushev, SYClausen, HNarimatsu, Yinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-29T15:16:19Zoai:repositorio-aberto.up.pt:10216/150450Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:19:27.825181Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Display of the human mucinome with defined O-glycans by gene engineered cells |
title |
Display of the human mucinome with defined O-glycans by gene engineered cells |
spellingShingle |
Display of the human mucinome with defined O-glycans by gene engineered cells Nason, R |
title_short |
Display of the human mucinome with defined O-glycans by gene engineered cells |
title_full |
Display of the human mucinome with defined O-glycans by gene engineered cells |
title_fullStr |
Display of the human mucinome with defined O-glycans by gene engineered cells |
title_full_unstemmed |
Display of the human mucinome with defined O-glycans by gene engineered cells |
title_sort |
Display of the human mucinome with defined O-glycans by gene engineered cells |
author |
Nason, R |
author_facet |
Nason, R Büll, C Konstantinidi, A Sun, L Ye, Z Halim, A Du, W Sørensen, DM Durbesson, F Furukawa, S Mandel, U Joshi, HJ Dworkin, LA Hansen, L David, L Iverson, TM Bensing, BA Sullam, PM Varki, A Vries, E Haan, CAM Vincentelli, R Henrissat, B Vakhrushev, SY Clausen, H Narimatsu, Y |
author_role |
author |
author2 |
Büll, C Konstantinidi, A Sun, L Ye, Z Halim, A Du, W Sørensen, DM Durbesson, F Furukawa, S Mandel, U Joshi, HJ Dworkin, LA Hansen, L David, L Iverson, TM Bensing, BA Sullam, PM Varki, A Vries, E Haan, CAM Vincentelli, R Henrissat, B Vakhrushev, SY Clausen, H Narimatsu, Y |
author2_role |
author author author author author author author author author author author author author author author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Nason, R Büll, C Konstantinidi, A Sun, L Ye, Z Halim, A Du, W Sørensen, DM Durbesson, F Furukawa, S Mandel, U Joshi, HJ Dworkin, LA Hansen, L David, L Iverson, TM Bensing, BA Sullam, PM Varki, A Vries, E Haan, CAM Vincentelli, R Henrissat, B Vakhrushev, SY Clausen, H Narimatsu, Y |
description |
Mucins are a large family of heavily O-glycosylated proteins that cover all mucosal surfaces and constitute the major macromolecules in most body fluids. Mucins are primarily defined by their variable tandem repeat (TR) domains that are densely decorated with different O-glycan structures in distinct patterns, and these arguably convey much of the informational content of mucins. Here, we develop a cell-based platform for the display and production of human TR O-glycodomains (~200 amino acids) with tunable structures and patterns of O-glycans using membrane-bound and secreted reporters expressed in glycoengineered HEK293 cells. Availability of defined mucin TR O-glycodomains advances experimental studies into the versatile role of mucins at the interface with pathogenic microorganisms and the microbiome, and sparks new strategies for molecular dissection of specific roles of adhesins, glycoside hydrolases, glycopeptidases, viruses and other interactions with mucin TRs as highlighted by examples. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021 2021-01-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://hdl.handle.net/10216/150450 |
url |
https://hdl.handle.net/10216/150450 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
2041-1723 10.1038/s41467-021-24366-4 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Nature Pub. Group |
publisher.none.fl_str_mv |
Nature Pub. Group |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799136112100245504 |