A post-translational modification of human Norovirus capsid protein attenuates glycan binding
| Autor: | Philipp H. O. Mayer, Charlotte Uetrecht, Thilo Stehle, Lena Lisbeth Grimm, Bärbel S. Blaum, Kasper D. Rand, Alvaro Mallagaray, Esben Trabjerg, Thomas Peters, Robert Creutznacher, Jose Maria Orduña, Jasmin Dülfer |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Models Molecular Protein Conformation alpha-Helical Polysaccharides/chemistry General Physics and Astronomy Gene Expression Recombinant Proteins/chemistry 02 engineering and technology Plasma protein binding medicine.disease_cause Crystallography X-Ray Norovirus/genetics Protein structure Isoaspartic Acid/chemistry Asparagine Cloning Molecular lcsh:Science Multidisciplinary Isoaspartic Acid biology Chemistry 021001 nanoscience & nanotechnology Recombinant Proteins 3. Good health Capsid Host-Pathogen Interactions Blood Group Antigens 0210 nano-technology Protein Binding Glycan Viral protein Science Genetic Vectors General Biochemistry Genetics and Molecular Biology Article Microbiology 03 medical and health sciences Antigen Polysaccharides medicine Escherichia coli Blood Group Antigens/chemistry Humans Protein Interaction Domains and Motifs Capsid Proteins/chemistry Binding site Binding Sites Asparagine/chemistry Norovirus General Chemistry Escherichia coli/genetics Kinetics 030104 developmental biology Genetic Vectors/chemistry biology.protein lcsh:Q Capsid Proteins Protein Conformation beta-Strand Protein Multimerization Protein Processing Post-Translational |
| Zdroj: | Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019) Nature Communications 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, vol. 10, no. 1, 1320 . https://doi.org/10.1038/s41467-019-09251-5 Nature Communications, 10 (1) |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-019-09251-5 |
| Popis: | 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. Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection. Here the authors report that an asparagine residue located near the HBGA-attachment site can convert into an iso-aspartate residue through spontaneous deamidation and influence HBGA recognition. |
| Databáze: | OpenAIRE |
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