Display of the human mucinome with defined O-glycans by gene engineered cells

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Display of the human mucinome with defined O-glycans by gene engineered cells. / Nason, Rebecca; Büll, Christian; Konstantinidi, Andriana; Sun, Lingbo; Ye, Zilu; Halim, Adnan; Du, Wenjuan; Sørensen, Daniel M.; Durbesson, Fabien; Furukawa, Sanae; Mandel, Ulla; Joshi, Hiren J.; Dworkin, Leo Alexander; Hansen, Lars; David, Leonor; Iverson, Tina M.; Bensing, Barbara A.; Sullam, Paul M.; Varki, Ajit; Vries, Erik de; de Haan, Cornelis A.M.; Vincentelli, Renaud; Henrissat, Bernard; Vakhrushev, Sergey Y.; Clausen, Henrik; Narimatsu, Yoshiki.

In: Nature Communications, Vol. 12, No. 1, 4070, 2021.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

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, ED, de Haan, CAM, Vincentelli, R, Henrissat, B, Vakhrushev, SY, Clausen, H & Narimatsu, Y 2021, 'Display of the human mucinome with defined O-glycans by gene engineered cells', Nature Communications, vol. 12, no. 1, 4070. https://doi.org/10.1038/s41467-021-24366-4

APA

Nason, R., Büll, C., Konstantinidi, A., Sun, L., Ye, Z., Halim, A., Du, W., Sørensen, D. M., Durbesson, F., Furukawa, S., Mandel, U., Joshi, H. J., Dworkin, L. A., Hansen, L., David, L., Iverson, T. M., Bensing, B. A., Sullam, P. M., Varki, A., ... Narimatsu, Y. (2021). Display of the human mucinome with defined O-glycans by gene engineered cells. Nature Communications, 12(1), [4070]. https://doi.org/10.1038/s41467-021-24366-4

Vancouver

Nason R, Büll C, Konstantinidi A, Sun L, Ye Z, Halim A et al. Display of the human mucinome with defined O-glycans by gene engineered cells. Nature Communications. 2021;12(1). 4070. https://doi.org/10.1038/s41467-021-24366-4

Author

Nason, Rebecca ; Büll, Christian ; Konstantinidi, Andriana ; Sun, Lingbo ; Ye, Zilu ; Halim, Adnan ; Du, Wenjuan ; Sørensen, Daniel M. ; Durbesson, Fabien ; Furukawa, Sanae ; Mandel, Ulla ; Joshi, Hiren J. ; Dworkin, Leo Alexander ; Hansen, Lars ; David, Leonor ; Iverson, Tina M. ; Bensing, Barbara A. ; Sullam, Paul M. ; Varki, Ajit ; Vries, Erik de ; de Haan, Cornelis A.M. ; Vincentelli, Renaud ; Henrissat, Bernard ; Vakhrushev, Sergey Y. ; Clausen, Henrik ; Narimatsu, Yoshiki. / Display of the human mucinome with defined O-glycans by gene engineered cells. In: Nature Communications. 2021 ; Vol. 12, No. 1.

Bibtex

@article{56e71d5490754c0ab4238014dd1cc498,

title = "Display of the human mucinome with defined O-glycans by gene engineered cells",

abstract = "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.",

author = "Rebecca Nason and Christian B{\"u}ll and Andriana Konstantinidi and Lingbo Sun and Zilu Ye and Adnan Halim and Wenjuan Du and S{\o}rensen, {Daniel M.} and Fabien Durbesson and Sanae Furukawa and Ulla Mandel and Joshi, {Hiren J.} and Dworkin, {Leo Alexander} and Lars Hansen and Leonor David and Iverson, {Tina M.} and Bensing, {Barbara A.} and Sullam, {Paul M.} and Ajit Varki and Vries, {Erik de} and {de Haan}, {Cornelis A.M.} and Renaud Vincentelli and Bernard Henrissat and Vakhrushev, {Sergey Y.} and Henrik Clausen and Yoshiki Narimatsu",

note = "Funding Information: This work was supported by the Lundbeck Foundation, the Novo Nordisk Foundation, the European Commission (GlycoImaging H2020-MSCA-ITN-721297, BioCapture H2020-MSCA-ITN-722171), the Danish National Research Foundation (DNRF107), the Mizutani Foundation (to Y.N.), the European Union{\textquoteright}s Horizon 2020 Research and Innovation Program under the Marie Sklodowska-Curie grant agreement No 787684 (to C.B.), and the National Institutes of Health grant (R01GM32373 to A.V. and GM137458 to T.M.I.). Publisher Copyright: {\textcopyright} 2021, The Author(s).",

year = "2021",

doi = "10.1038/s41467-021-24366-4",

language = "English",

volume = "12",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "nature publishing group",

number = "1",

}

RIS

TY - JOUR

T1 - Display of the human mucinome with defined O-glycans by gene engineered cells

AU - Nason, Rebecca

AU - Büll, Christian

AU - Konstantinidi, Andriana

AU - Sun, Lingbo

AU - Ye, Zilu

AU - Halim, Adnan

AU - Du, Wenjuan

AU - Sørensen, Daniel M.

AU - Durbesson, Fabien

AU - Furukawa, Sanae

AU - Mandel, Ulla

AU - Joshi, Hiren J.

AU - Dworkin, Leo Alexander

AU - Hansen, Lars

AU - David, Leonor

AU - Iverson, Tina M.

AU - Bensing, Barbara A.

AU - Sullam, Paul M.

AU - Varki, Ajit

AU - Vries, Erik de

AU - de Haan, Cornelis A.M.

AU - Vincentelli, Renaud

AU - Henrissat, Bernard

AU - Vakhrushev, Sergey Y.

AU - Clausen, Henrik

AU - Narimatsu, Yoshiki

N1 - Funding Information: This work was supported by the Lundbeck Foundation, the Novo Nordisk Foundation, the European Commission (GlycoImaging H2020-MSCA-ITN-721297, BioCapture H2020-MSCA-ITN-722171), the Danish National Research Foundation (DNRF107), the Mizutani Foundation (to Y.N.), the European Union’s Horizon 2020 Research and Innovation Program under the Marie Sklodowska-Curie grant agreement No 787684 (to C.B.), and the National Institutes of Health grant (R01GM32373 to A.V. and GM137458 to T.M.I.). Publisher Copyright: © 2021, The Author(s).

PY - 2021

Y1 - 2021

N2 - 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.

AB - 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.

U2 - 10.1038/s41467-021-24366-4

DO - 10.1038/s41467-021-24366-4

M3 - Journal article

C2 - 34210959

AN - SCOPUS:85109164107

VL - 12

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 4070

ER -

ID: 274573616