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TitleSecreted dengue virus NS1 from infection is predominantly dimeric and in complex with high-density lipoprotein.
Journal, issue, pagesElife, Vol. 12, Year 2024
Publish dateMay 24, 2024
AuthorsBing Liang Alvin Chew / A N Qi Ngoh / Wint Wint Phoo / Kitti Wing Ki Chan / Zheng Ser / Nikhil K Tulsian / Shiao See Lim / Mei Jie Grace Weng / Satoru Watanabe / Milly M Choy / Jenny Low / Eng Eong Ooi / Christiane Ruedl / Radoslaw M Sobota / Subhash G Vasudevan / Dahai Luo /
PubMed AbstractSevere dengue infections are characterized by endothelial dysfunction shown to be associated with the secreted nonstructural protein 1 (sNS1), making it an attractive vaccine antigen and ...Severe dengue infections are characterized by endothelial dysfunction shown to be associated with the secreted nonstructural protein 1 (sNS1), making it an attractive vaccine antigen and biotherapeutic target. To uncover the biologically relevant structure of sNS1, we obtained infection-derived sNS1 (isNS1) from dengue virus (DENV)-infected Vero cells through immunoaffinity purification instead of recombinant sNS1 (rsNS1) overexpressed in insect or mammalian cell lines. We found that isNS1 appeared as an approximately 250 kDa complex of NS1 and ApoA1 and further determined the cryoEM structures of isNS1 and its complex with a monoclonal antibody/Fab. Indeed, we found that the major species of isNS1 is a complex of the NS1 dimer partially embedded in a high-density lipoprotein (HDL) particle. Crosslinking mass spectrometry studies confirmed that the isNS1 interacts with the major HDL component ApoA1 through interactions that map to the NS1 wing and hydrophobic domains. Furthermore, our studies demonstrated that the sNS1 in sera from DENV-infected mice and a human patient form a similar complex as isNS1. Our results report the molecular architecture of a biological form of sNS1, which may have implications for the molecular pathogenesis of dengue.
External linksElife / PubMed:38787378 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 3.8 Å
Structure data

EMDB-36480: CryoEM structure of isNS1 in complex with Fab56.2 and HDL
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-36483: CryoEM structure of isNS1 in complex with Fab56.2
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • dengue virus type 2
  • Mus musculus (house mouse)

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