Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis of Zika virus NS1 multimerization and human antibody recognition.
Journal, issue, pages	Npj Viruses, Vol. 2, Issue 1, Page 14, Year 2024
Publish date	Apr 25, 2024
Authors	Bing Liang Alvin Chew / An Qi Ngoh / Wint Wint Phoo / Mei Jie Grace Weng / Ho Jun Sheng / Kitti Wing Ki Chan / Eddie Yong Jun Tan / Terri Gelbart / Chenrui Xu / Gene S Tan / Subhash G Vasudevan / Dahai Luo /
PubMed Abstract	Zika virus (ZIKV) belongs to the Flavivirus genus of the Flaviviridae family along with the four serotypes of dengue virus (DENV1-4). The recent global outbreaks of contemporary ZIKV strains ...Zika virus (ZIKV) belongs to the Flavivirus genus of the Flaviviridae family along with the four serotypes of dengue virus (DENV1-4). The recent global outbreaks of contemporary ZIKV strains demonstrated that infection can lead to neurological sequelae in adults and severe abnormalities in newborns that were previously unreported with ancestral strains. As such, there remains an unmet need for efficacious vaccines and antiviral agents against ZIKV. The non-structural protein 1 (NS1) is secreted from the infected cell and is thought to be associated with disease severity besides its proven usefulness for differential diagnoses. However, its physiologically relevant structure and pathogenesis mechanisms remain unclear. Here, we present high-resolution cryoEM structures of ZIKV recombinant secreted NS1 (rsNS1) and its complexes with three human monoclonal antibodies (AA12, EB9, GB5), as well as evidence for ZIKV infection-derived secreted NS1 (isNS1) binding to High Density Lipoprotein (HDL). We show that ZIKV rsNS1 forms tetramers and filamentous repeats of tetramers. We also observed that antibody binding did not disrupt the ZIKV NS1 tetramers as they bound to the wing and connector subdomain of the β-ladder. Our study reveals new insights into NS1 multimerization, highlights the need to distinguish the polymorphic nature of rsNS1 and isNS1, and expands the mechanistic basis of the protection conferred by antibodies targeting NS1.
External links	Npj Viruses / PubMed:40295651 / PubMed Central
Methods	EM (single particle) / EM (helical sym.)
Resolution	2.8 - 8.0 Å
Structure data	37663 8wn8 EMDB-37663, PDB-8wn8: CryoEM structure of ZIKV rsNS1 Method: EM (single particle) / Resolution: 3.0 Å 37670 8wnp EMDB-37670, PDB-8wnp: ZIKV rsNS1 in complex with Fab AA12 and anti-fab nanobody Method: EM (single particle) / Resolution: 3.1 Å 37673 8wnu EMDB-37673, PDB-8wnu: ZIKV rsNS1 in complex with Fab GB5 and anti-fab nanobody Method: EM (single particle) / Resolution: 3.8 Å 37676 8wo0 EMDB-37676, PDB-8wo0: CryoEM structure of ZIKV rsNS1 filament Method: EM (helical sym.) / Resolution: 8.0 Å 37678 8wo4 EMDB-37678, PDB-8wo4: ZIKV rsNS1 in complex with Fab EB9 and anti-fab nanobody Method: EM (single particle) / Resolution: 2.8 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose
Source	zika virus homo sapiens (human) lama glama (llama)
Keywords	VIRAL PROTEIN / Flavivirus / ZIKA / NS1 / VIRAL PROTEIN/IMMUNE SYSTEM / antibody / cryoEM / non structural protein 1 / VIRAL PROTEIN-IMMUNE SYSTEM complex