دورية أكاديمية
أعرض في EDS

Secreted dengue virus NS1 from infection is predominantly dimeric and in complex with high-density lipoprotein.

التفاصيل البيبلوغرافية
العنوان: Secreted dengue virus NS1 from infection is predominantly dimeric and in complex with high-density lipoprotein.
المؤلفون: Chew BLA; Lee Kong Chian School of Medicine, Nanyang Technological University, Singapore, Singapore.; NTU Institute of Structural Biology, Nanyang Technological University, Singapore, Singapore., Ngoh ANQ; Program in Emerging Infectious Diseases, Duke-NUS Medical School, Singapore, Singapore., Phoo WW; Functional Proteomics Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research, Singapore, Singapore., Chan KWK; Program in Emerging Infectious Diseases, Duke-NUS Medical School, Singapore, Singapore., Ser Z; Functional Proteomics Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research, Singapore, Singapore., Tulsian NK; Department of Biological Sciences, National University of Singapore, Singapore, Singapore.; Singapore Centre for Life Sciences, Department of Biochemistry, National University of Singapore, Singapore, Singapore., Lim SS; Program in Emerging Infectious Diseases, Duke-NUS Medical School, Singapore, Singapore., Weng MJG; Lee Kong Chian School of Medicine, Nanyang Technological University, Singapore, Singapore.; NTU Institute of Structural Biology, Nanyang Technological University, Singapore, Singapore., Watanabe S; Program in Emerging Infectious Diseases, Duke-NUS Medical School, Singapore, Singapore., Choy MM; Program in Emerging Infectious Diseases, Duke-NUS Medical School, Singapore, Singapore., Low J; Program in Emerging Infectious Diseases, Duke-NUS Medical School, Singapore, Singapore.; Department of Infectious Diseases, Singapore General Hospital, Singapore, Singapore., Ooi EE; Program in Emerging Infectious Diseases, Duke-NUS Medical School, Singapore, Singapore.; Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.; Saw Swee Hock School of Public Health, National University of Singapore, Singapore, Singapore., Ruedl C; School of Biological Sciences, Nanyang Technological University, Singapore, Singapore., Sobota RM; Functional Proteomics Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research, Singapore, Singapore., Vasudevan SG; Program in Emerging Infectious Diseases, Duke-NUS Medical School, Singapore, Singapore.; Department of Microbiology and Immunology, National University of Singapore, Singapore, Singapore.; Institute for Glycomics (G26), Griffith University Gold Coast Campus, Southport, Australia., Luo D; Lee Kong Chian School of Medicine, Nanyang Technological University, Singapore, Singapore.; NTU Institute of Structural Biology, Nanyang Technological University, Singapore, Singapore.
المصدر: ELife [Elife] 2024 May 24; Vol. 12. Date of Electronic Publication: 2024 May 24.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: Viral Nonstructural Proteins*/metabolism , Viral Nonstructural Proteins*/chemistry , Viral Nonstructural Proteins*/genetics , Dengue Virus*/genetics , Dengue Virus*/metabolism , Lipoproteins, HDL*/metabolism , Dengue*/virology , Dengue*/metabolism, Animals ; Chlorocebus aethiops ; Mice ; Humans ; Vero Cells ; Apolipoprotein A-I/metabolism ; Apolipoprotein A-I/chemistry ; Protein Multimerization ; Cryoelectron Microscopy
مستخلص: 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.
Competing Interests: BC, AN, WP, KC, ZS, NT, SL, MW, SW, MC, JL, EO, CR, RS, SV, DL No competing interests declared
(© 2023, Chew, Ngoh, Phoo et al.)
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معلومات مُعتمدة: T2EP30220-0020 Ministry of Education - Singapore; MOH-OFIRG20nov-0002 National Medical Research Council; LKCMedicine Dean's Postdoctoral Fellowship Lee Kong Chian School of Medicine, Nanyang Technological University; MOHOFIRG18may-0006 National Medical Research Council; Career Development Fund 2021 Agency for Science, Technology and Research
فهرسة مساهمة: Keywords: biomarker; cryoEM; dengue infection; flavivirus; high-density lipoprotein; human; infectious disease; microbiology; molecular biophysics; mouse; pathogenesis factor; structural biology
المشرفين على المادة: 0 (Viral Nonstructural Proteins)
0 (Lipoproteins, HDL)
0 (Apolipoprotein A-I)
0 (NS1 protein, dengue-1 virus)
0 (NS1 protein, Dengue virus type 2)
تواريخ الأحداث: Date Created: 20240524 Date Completed: 20240524 Latest Revision: 20240526
رمز التحديث: 20240526
مُعرف محوري في PubMed: PMC11126310
DOI: 10.7554/eLife.90762
PMID: 38787378
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.90762