A post-translational modification of human Norovirus capsid protein attenuates glycan binding

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

Standard

A post-translational modification of human Norovirus capsid protein attenuates glycan binding. / Mallagaray, Alvaro; Creutznacher, Robert; Dülfer, Jasmin; Mayer, Philipp H O; Grimm, Lena Lisbeth; Orduña, Jose Maria; Trabjerg, Esben; Stehle, Thilo; Rand, Kasper D; Blaum, Bärbel S; Uetrecht, Charlotte; Peters, Thomas.

In: Nature Communications, Vol. 10, No. 1, 1320, 21.03.2019.

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

Harvard

Mallagaray, A, Creutznacher, R, Dülfer, J, Mayer, PHO, Grimm, LL, Orduña, JM, Trabjerg, E, Stehle, T, Rand, KD, Blaum, BS, Uetrecht, C & Peters, T 2019, 'A post-translational modification of human Norovirus capsid protein attenuates glycan binding', Nature Communications, vol. 10, no. 1, 1320. https://doi.org/10.1038/s41467-019-09251-5

APA

Mallagaray, A., Creutznacher, R., Dülfer, J., Mayer, P. H. O., Grimm, L. L., Orduña, J. M., Trabjerg, E., Stehle, T., Rand, K. D., Blaum, B. S., Uetrecht, C., & Peters, T. (2019). A post-translational modification of human Norovirus capsid protein attenuates glycan binding. Nature Communications, 10(1), [1320]. https://doi.org/10.1038/s41467-019-09251-5

Vancouver

Mallagaray A, Creutznacher R, Dülfer J, Mayer PHO, Grimm LL, Orduña JM et al. A post-translational modification of human Norovirus capsid protein attenuates glycan binding. Nature Communications. 2019 Mar 21;10(1). 1320. https://doi.org/10.1038/s41467-019-09251-5

Author

Mallagaray, Alvaro ; Creutznacher, Robert ; Dülfer, Jasmin ; Mayer, Philipp H O ; Grimm, Lena Lisbeth ; Orduña, Jose Maria ; Trabjerg, Esben ; Stehle, Thilo ; Rand, Kasper D ; Blaum, Bärbel S ; Uetrecht, Charlotte ; Peters, Thomas. / A post-translational modification of human Norovirus capsid protein attenuates glycan binding. In: Nature Communications. 2019 ; Vol. 10, No. 1.

Bibtex

@article{314f8a4afcb54db4afa4bb3806550686,
title = "A post-translational modification of human Norovirus capsid protein attenuates glycan binding",
abstract = "Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employ protein NMR experiments supported by mass spectrometry and crystallography to study HBGA binding to the P-domain of a prevalent virus strain (GII.4). We report a highly selective transformation of asparagine 373, located in an antigenic loop adjoining the HBGA binding site, into an iso-aspartate residue. This spontaneous post-translational modification (PTM) proceeds with an estimated half-life of a few days at physiological temperatures, independent of the presence of HBGAs but dramatically affecting HBGA recognition. Sequence conservation and the surface-exposed position of this PTM suggest an important role in infection and immune recognition for many norovirus strains.",
keywords = "Asparagine/chemistry, Binding Sites, Blood Group Antigens/chemistry, Capsid Proteins/chemistry, Cloning, Molecular, Crystallography, X-Ray, Escherichia coli/genetics, Gene Expression, Genetic Vectors/chemistry, Host-Pathogen Interactions, Humans, Isoaspartic Acid/chemistry, Kinetics, Models, Molecular, Norovirus/genetics, Polysaccharides/chemistry, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Processing, Post-Translational, Recombinant Proteins/chemistry",
author = "Alvaro Mallagaray and Robert Creutznacher and Jasmin D{\"u}lfer and Mayer, {Philipp H O} and Grimm, {Lena Lisbeth} and Ordu{\~n}a, {Jose Maria} and Esben Trabjerg and Thilo Stehle and Rand, {Kasper D} and Blaum, {B{\"a}rbel S} and Charlotte Uetrecht and Thomas Peters",
year = "2019",
month = mar,
day = "21",
doi = "10.1038/s41467-019-09251-5",
language = "English",
volume = "10",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - A post-translational modification of human Norovirus capsid protein attenuates glycan binding

AU - Mallagaray, Alvaro

AU - Creutznacher, Robert

AU - Dülfer, Jasmin

AU - Mayer, Philipp H O

AU - Grimm, Lena Lisbeth

AU - Orduña, Jose Maria

AU - Trabjerg, Esben

AU - Stehle, Thilo

AU - Rand, Kasper D

AU - Blaum, Bärbel S

AU - Uetrecht, Charlotte

AU - Peters, Thomas

PY - 2019/3/21

Y1 - 2019/3/21

N2 - Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employ protein NMR experiments supported by mass spectrometry and crystallography to study HBGA binding to the P-domain of a prevalent virus strain (GII.4). We report a highly selective transformation of asparagine 373, located in an antigenic loop adjoining the HBGA binding site, into an iso-aspartate residue. This spontaneous post-translational modification (PTM) proceeds with an estimated half-life of a few days at physiological temperatures, independent of the presence of HBGAs but dramatically affecting HBGA recognition. Sequence conservation and the surface-exposed position of this PTM suggest an important role in infection and immune recognition for many norovirus strains.

AB - Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employ protein NMR experiments supported by mass spectrometry and crystallography to study HBGA binding to the P-domain of a prevalent virus strain (GII.4). We report a highly selective transformation of asparagine 373, located in an antigenic loop adjoining the HBGA binding site, into an iso-aspartate residue. This spontaneous post-translational modification (PTM) proceeds with an estimated half-life of a few days at physiological temperatures, independent of the presence of HBGAs but dramatically affecting HBGA recognition. Sequence conservation and the surface-exposed position of this PTM suggest an important role in infection and immune recognition for many norovirus strains.

KW - Asparagine/chemistry

KW - Binding Sites

KW - Blood Group Antigens/chemistry

KW - Capsid Proteins/chemistry

KW - Cloning, Molecular

KW - Crystallography, X-Ray

KW - Escherichia coli/genetics

KW - Gene Expression

KW - Genetic Vectors/chemistry

KW - Host-Pathogen Interactions

KW - Humans

KW - Isoaspartic Acid/chemistry

KW - Kinetics

KW - Models, Molecular

KW - Norovirus/genetics

KW - Polysaccharides/chemistry

KW - Protein Binding

KW - Protein Conformation, alpha-Helical

KW - Protein Conformation, beta-Strand

KW - Protein Interaction Domains and Motifs

KW - Protein Multimerization

KW - Protein Processing, Post-Translational

KW - Recombinant Proteins/chemistry

U2 - 10.1038/s41467-019-09251-5

DO - 10.1038/s41467-019-09251-5

M3 - Journal article

C2 - 30899001

VL - 10

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 1320

ER -

ID: 216348533