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Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry

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Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry. / Jae, Lucas T; Raaben, Matthijs; Riemersma, Moniek; van Beusekom, Ellen; Blomen, Vincent A; Velds, Arno; Kerkhoven, Ron M; Carette, Jan E; Topaloglu, Haluk; Meinecke, Peter; Wessels, Marja W; Lefeber, Dirk J; Whelan, Sean P; van Bokhoven, Hans; Brummelkamp, Thijn R.

In: SCIENCE, Vol. 340, No. 6131, 26.04.2013, p. 479-83.

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

Harvard

Jae, LT, Raaben, M, Riemersma, M, van Beusekom, E, Blomen, VA, Velds, A, Kerkhoven, RM, Carette, JE, Topaloglu, H, Meinecke, P, Wessels, MW, Lefeber, DJ, Whelan, SP, van Bokhoven, H & Brummelkamp, TR 2013, 'Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry', SCIENCE, vol. 340, no. 6131, pp. 479-83. https://doi.org/10.1126/science.1233675

APA

Jae, L. T., Raaben, M., Riemersma, M., van Beusekom, E., Blomen, V. A., Velds, A., Kerkhoven, R. M., Carette, J. E., Topaloglu, H., Meinecke, P., Wessels, M. W., Lefeber, D. J., Whelan, S. P., van Bokhoven, H., & Brummelkamp, T. R. (2013). Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry. SCIENCE, 340(6131), 479-83. https://doi.org/10.1126/science.1233675

Vancouver

Jae LT, Raaben M, Riemersma M, van Beusekom E, Blomen VA, Velds A et al. Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry. SCIENCE. 2013 Apr 26;340(6131):479-83. https://doi.org/10.1126/science.1233675

Bibtex

@article{13d295c58ff04036bd4e81a9ca6bb968,
title = "Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry",
abstract = "Glycosylated α-dystroglycan (α-DG) serves as cellular entry receptor for multiple pathogens, and defects in its glycosylation cause hereditary Walker-Warburg syndrome (WWS). At least eight proteins are critical to glycosylate α-DG, but many genes mutated in WWS remain unknown. To identify modifiers of α-DG, we performed a haploid screen for Lassa virus entry, a hemorrhagic fever virus causing thousands of deaths annually that hijacks glycosylated α-DG to enter cells. In complementary screens, we profiled cells for absence of α-DG carbohydrate chains or biochemically related glycans. This revealed virus host factors and a suite of glycosylation units, including all known Walker-Warburg genes and five additional factors critical for the modification of α-DG. Our findings accentuate the complexity of this posttranslational feature and point out genes defective in dystroglycanopathies.",
keywords = "Amino Acid Sequence, Cell Line, Dystroglycans, Female, Glycosylation, Haploidy, Host-Pathogen Interactions, Humans, Infant, Lassa Fever, Lassa virus, Male, Membrane Proteins, Molecular Sequence Data, Mutation, Pedigree, Proteome, Virus Internalization, Walker-Warburg Syndrome",
author = "Jae, {Lucas T} and Matthijs Raaben and Moniek Riemersma and {van Beusekom}, Ellen and Blomen, {Vincent A} and Arno Velds and Kerkhoven, {Ron M} and Carette, {Jan E} and Haluk Topaloglu and Peter Meinecke and Wessels, {Marja W} and Lefeber, {Dirk J} and Whelan, {Sean P} and {van Bokhoven}, Hans and Brummelkamp, {Thijn R}",
year = "2013",
month = apr,
day = "26",
doi = "10.1126/science.1233675",
language = "English",
volume = "340",
pages = "479--83",
journal = "SCIENCE",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6131",

}

RIS

TY - JOUR

T1 - Deciphering the glycosylome of dystroglycanopathies using haploid screens for lassa virus entry

AU - Jae, Lucas T

AU - Raaben, Matthijs

AU - Riemersma, Moniek

AU - van Beusekom, Ellen

AU - Blomen, Vincent A

AU - Velds, Arno

AU - Kerkhoven, Ron M

AU - Carette, Jan E

AU - Topaloglu, Haluk

AU - Meinecke, Peter

AU - Wessels, Marja W

AU - Lefeber, Dirk J

AU - Whelan, Sean P

AU - van Bokhoven, Hans

AU - Brummelkamp, Thijn R

PY - 2013/4/26

Y1 - 2013/4/26

N2 - Glycosylated α-dystroglycan (α-DG) serves as cellular entry receptor for multiple pathogens, and defects in its glycosylation cause hereditary Walker-Warburg syndrome (WWS). At least eight proteins are critical to glycosylate α-DG, but many genes mutated in WWS remain unknown. To identify modifiers of α-DG, we performed a haploid screen for Lassa virus entry, a hemorrhagic fever virus causing thousands of deaths annually that hijacks glycosylated α-DG to enter cells. In complementary screens, we profiled cells for absence of α-DG carbohydrate chains or biochemically related glycans. This revealed virus host factors and a suite of glycosylation units, including all known Walker-Warburg genes and five additional factors critical for the modification of α-DG. Our findings accentuate the complexity of this posttranslational feature and point out genes defective in dystroglycanopathies.

AB - Glycosylated α-dystroglycan (α-DG) serves as cellular entry receptor for multiple pathogens, and defects in its glycosylation cause hereditary Walker-Warburg syndrome (WWS). At least eight proteins are critical to glycosylate α-DG, but many genes mutated in WWS remain unknown. To identify modifiers of α-DG, we performed a haploid screen for Lassa virus entry, a hemorrhagic fever virus causing thousands of deaths annually that hijacks glycosylated α-DG to enter cells. In complementary screens, we profiled cells for absence of α-DG carbohydrate chains or biochemically related glycans. This revealed virus host factors and a suite of glycosylation units, including all known Walker-Warburg genes and five additional factors critical for the modification of α-DG. Our findings accentuate the complexity of this posttranslational feature and point out genes defective in dystroglycanopathies.

KW - Amino Acid Sequence

KW - Cell Line

KW - Dystroglycans

KW - Female

KW - Glycosylation

KW - Haploidy

KW - Host-Pathogen Interactions

KW - Humans

KW - Infant

KW - Lassa Fever

KW - Lassa virus

KW - Male

KW - Membrane Proteins

KW - Molecular Sequence Data

KW - Mutation

KW - Pedigree

KW - Proteome

KW - Virus Internalization

KW - Walker-Warburg Syndrome

U2 - 10.1126/science.1233675

DO - 10.1126/science.1233675

M3 - SCORING: Journal article

C2 - 23519211

VL - 340

SP - 479

EP - 483

JO - SCIENCE

JF - SCIENCE

SN - 0036-8075

IS - 6131

ER -