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

doi:10.1038/ncomms14438

GSTDTAP > 资源环境科学

DOI	10.1038/ncomms14438
	A post-translational modification of human Norovirus capsid protein attenuates glycan binding
	Mallagaray, Alvaro 1; Creutznacher, Robert 1; Duelfer, Jasmin 2; Mayer, Philipp H. O.3; Grimm, Lena Lisbeth 1; Orduna, Jose Maria 1,6; Trabjerg, Esben 4,7; Stehle, Thilo 3; Rand, Kasper D.4; Blaum, Baerbel S.3; Uetrecht, Charlotte 2,5; Peters, Thomas 1
	2019-03-21
发表期刊	NATURE COMMUNICATIONS
ISSN	2041-1723
出版年	2019
卷号	10
文章类型	Article
语种	英语
国家	Germany; Denmark; Spain; Switzerland
英文摘要	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.
领域	资源环境
收录类别	SCI-E
WOS记录号	WOS:000461881700025
WOS关键词	BLOOD-GROUP ANTIGENS ; CRYSTAL-STRUCTURES ; NMR-SPECTROSCOPY ; STRUCTURAL BASIS ; DEAMIDATION ; PEPTIDES ; ISOMERIZATION ; SUCCINIMIDE ; ASSIGNMENT ; COMPLEX
WOS类目	Multidisciplinary Sciences
WOS研究方向	Science & Technology - Other Topics
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引用统计
文献类型	期刊论文
条目标识符	http://119.78.100.173/C666/handle/2XK7JSWQ/203242
专题	资源环境科学
作者单位	1.Univ Lubeck, Inst Chem & Metabol, Ctr Struct & Cell Biol Med CSCM, Ratzeburger Allee 160, D-23562 Lubeck, Germany; 2.Leibniz Inst Expt Virol, Heinrich Pette Inst, Martinistr 52, D-20251 Hamburg, Germany; 3.Univ Tubingen, Interfac Inst Biochem, Hoppe Seyler Str 4, D-72076 Tubingen, Germany; 4.Univ Copenhagen, Dept Pharm, Univ Pk 2, DK-2100 Copenhagen, Denmark; 5.European XFEL GmbH, Holzkoppel 4, D-22869 Schenefeld, Germany; 6.San Pablo CEU Univ, Inst Chem, Fac Pharm, Boadilla Del Monte 28668, Spain; 7.Swiss Fed Inst Technol, Inst Mol Syst Biol, Zurich, Switzerland
推荐引用方式 GB/T 7714	Mallagaray, Alvaro,Creutznacher, Robert,Duelfer, Jasmin,et al. A post-translational modification of human Norovirus capsid protein attenuates glycan binding[J]. NATURE COMMUNICATIONS,2019,10.
APA	Mallagaray, Alvaro.,Creutznacher, Robert.,Duelfer, Jasmin.,Mayer, Philipp H. O..,Grimm, Lena Lisbeth.,...&Peters, Thomas.(2019).A post-translational modification of human Norovirus capsid protein attenuates glycan binding.NATURE COMMUNICATIONS,10.
MLA	Mallagaray, Alvaro,et al."A post-translational modification of human Norovirus capsid protein attenuates glycan binding".NATURE COMMUNICATIONS 10(2019).