Home > Publications database > Nonstructural protein 4 of human norovirus self-assembles into various membrane-bridging multimers. > print

001     292524
005     20241002155845.0
024 7 _ |a 10.1016/j.jbc.2024.107724
|2 doi
024 7 _ |a pmid:39214299
|2 pmid
024 7 _ |a 0021-9258
|2 ISSN
024 7 _ |a 1067-8816
|2 ISSN
024 7 _ |a 1083-351X
|2 ISSN
037 _ _ |a DKFZ-2024-01770
041 _ _ |a English
082 _ _ |a 540
100 1 _ |a Royet, Adrien
|b 0
245 _ _ |a Nonstructural protein 4 of human norovirus self-assembles into various membrane-bridging multimers.
260 _ _ |a Bethesda, Md.
|c 2024
|b Soc.
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|s 1727877488_24786
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
500 _ _ |a Volume 300, Issue 9, September 2024, 107724 / Core Facility Antibodies
520 _ _ |a Single-stranded, positive-sense RNA ((+)RNA) viruses replicate their genomes in virus-induced intracellular membrane compartments. (+)RNA viruses dedicate a significant part of their small genomes (a few thousands to a few tens of thousands of bases) to the generation of these compartments by encoding membrane-interacting proteins and/or protein domains. Noroviruses are a very diverse genus of (+)RNA viruses including human and animal pathogens. Human noroviruses are the major cause of acute gastroenteritis worldwide, with genogroup II genotype 4 (GII.4) noroviruses accounting for the vast majority of infections. Three viral proteins encoded in the N-terminus of the viral replication polyprotein direct intracellular membrane rearrangements associated with norovirus replication. Of these three, nonstructural protein 4 (NS4) seems to be the most important, although its exact functions in replication organelle formation are unknown. Here we produce, purify and characterize GII.4 NS4. AlphaFold modeling combined with experimental data refine and correct our previous crude structural model of NS4. Using simple artificial liposomes, we report an extensive characterization of the membrane properties of NS4. We find that NS4 self-assembles and thereby bridges liposomes together. Cryo-EM, NMR and membrane flotation show formation of several distinct NS4 assemblies, at least two of them bridging pairs of membranes together in different fashions. Noroviruses belong to (+)RNA viruses whose replication compartment is extruded from the target endomembrane and generates double-membrane vesicles. Our data establish that the 21-kDa GII.4 human norovirus NS4 can, in the absence of any other factor, recapitulate in tubo several features, including membrane apposition, that occur in such processes.
536 _ _ |a 311 - Zellbiologie und Tumorbiologie (POF4-311)
|0 G:(DE-HGF)POF4-311
|c POF4-311
|f POF IV
|x 0
588 _ _ |a Dataset connected to CrossRef, PubMed, , Journals: inrepo02.dkfz.de
650 _ 7 |a Cryo-electron microscopy
|2 Other
650 _ 7 |a Lipid-protein interaction
|2 Other
650 _ 7 |a Liposome
|2 Other
650 _ 7 |a Membrane
|2 Other
650 _ 7 |a Nonstructural protein
|2 Other
650 _ 7 |a Norovirus
|2 Other
650 _ 7 |a Plus-stranded RNA virus
|2 Other
650 _ 7 |a Protein assembly
|2 Other
650 _ 7 |a Viral protein
|2 Other
650 _ 7 |a Viral replication
|2 Other
700 1 _ |a Ruedas, Rémi
|b 1
700 1 _ |a Gargowitsch, Laetitia
|b 2
700 1 _ |a Gervais, Virginie
|b 3
700 1 _ |a Habersetzer, Johann
|b 4
700 1 _ |a Pieri, Laura
|b 5
700 1 _ |a Ouldali, Malika
|b 6
700 1 _ |a Paternostre, Maïté
|b 7
700 1 _ |a Hofmann, Ilse
|0 P:(DE-He78)0c4543046185361a644540fee0dad8b1
|b 8
|u dkfz
700 1 _ |a Tubiana, Thibault
|b 9
700 1 _ |a Fieulaine, Sonia
|b 10
700 1 _ |a Bressanelli, Stéphane
|b 11
773 _ _ |a 10.1016/j.jbc.2024.107724
|g p. 107724 -
|0 PERI:(DE-600)1474604-9
|p 107724
|t The journal of biological chemistry
|v 300
|y 2024
|x 0021-9258
909 C O |p VDB
|o oai:inrepo02.dkfz.de:292524
910 1 _ |a Deutsches Krebsforschungszentrum
|0 I:(DE-588b)2036810-0
|k DKFZ
|b 8
|6 P:(DE-He78)0c4543046185361a644540fee0dad8b1
913 1 _ |a DE-HGF
|b Gesundheit
|l Krebsforschung
|1 G:(DE-HGF)POF4-310
|0 G:(DE-HGF)POF4-311
|3 G:(DE-HGF)POF4
|2 G:(DE-HGF)POF4-300
|4 G:(DE-HGF)POF
|v Zellbiologie und Tumorbiologie
|x 0
914 1 _ |y 2024
915 _ _ |a JCR
|0 StatID:(DE-HGF)0100
|2 StatID
|b J BIOL CHEM : 2019
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0200
|2 StatID
|b SCOPUS
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0300
|2 StatID
|b Medline
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0320
|2 StatID
|b PubMed Central
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0600
|2 StatID
|b Ebsco Academic Search
|d 2021-05-04
915 _ _ |a Peer Review
|0 StatID:(DE-HGF)0030
|2 StatID
|b ASC
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0199
|2 StatID
|b Clarivate Analytics Master Journal List
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1030
|2 StatID
|b Current Contents - Life Sciences
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0160
|2 StatID
|b Essential Science Indicators
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1050
|2 StatID
|b BIOSIS Previews
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1190
|2 StatID
|b Biological Abstracts
|d 2021-05-04
915 _ _ |a WoS
|0 StatID:(DE-HGF)0113
|2 StatID
|b Science Citation Index Expanded
|d 2021-05-04
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0150
|2 StatID
|b Web of Science Core Collection
|d 2021-05-04
915 _ _ |a IF < 5
|0 StatID:(DE-HGF)9900
|2 StatID
|d 2021-05-04
920 1 _ |0 I:(DE-He78)A190-20160331
|k A190
|l A190 Vaskuläre Onkologie und Metastasierung
|x 0
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a I:(DE-He78)A190-20160331
980 _ _ |a UNRESTRICTED

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21