دورية أكاديمية
أعرض في EDS

Mapping of molecular interactions between human E3 ligase TRIM69 and Dengue virus NS3 protease using hydrogen-deuterium exchange mass spectrometry.

التفاصيل البيبلوغرافية
العنوان: Mapping of molecular interactions between human E3 ligase TRIM69 and Dengue virus NS3 protease using hydrogen-deuterium exchange mass spectrometry.
المؤلفون: Bagga T; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore., Tulsian NK; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore. nikhil.tulsian@nus.edu.sg.; Department of Biochemistry, National University of Singapore, 28 Medical Drive, Singapore, 117546, Singapore. nikhil.tulsian@nus.edu.sg., Mok YK; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore., Kini RM; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore.; Department of Pharmacology, Yong Loo Lin School of Medicine, National University of Singapore, 16 Medical Drive, Singapore, 117600, Singapore.; Department of Biochemistry and Molecular Biology, Virginia Commonwealth University, 1101 E Marshall Street, Richmond, VA, 23298, USA., Sivaraman J; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore. dbsjayar@nus.edu.sg.
المصدر: Cellular and molecular life sciences : CMLS [Cell Mol Life Sci] 2022 Apr 10; Vol. 79 (5), pp. 233. Date of Electronic Publication: 2022 Apr 10.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Springer Country of Publication: Switzerland NLM ID: 9705402 Publication Model: Electronic Cited Medium: Internet ISSN: 1420-9071 (Electronic) Linking ISSN: 1420682X NLM ISO Abbreviation: Cell Mol Life Sci Subsets: MEDLINE
أسماء مطبوعة: Publication: Basel : Springer
Original Publication: Basel ; Boston : Birkhauser, c1997-
مواضيع طبية MeSH: Dengue Virus*/physiology , Serine Endopeptidases*/chemistry , Tripartite Motif Proteins*/chemistry , Ubiquitin-Protein Ligases*/chemistry , Viral Nonstructural Proteins*/chemistry, Dengue ; Deuterium Exchange Measurement ; Humans ; Mass Spectrometry
مستخلص: Tripartite motif (TRIM) E3 ligases target specific substrates, including viral proteins, for proteasomal degradation, and are thus essential regulators of the innate antiviral response. TRIM69 ubiquitinates the non-structural NS3 protein of Dengue virus for its degradation by the host machinery. This antiviral strategy abrogates the immunosuppression mediated by the NS2B-NS3 protease complex. To understand how this host-driven antiviral response against Dengue virus, we sought to define the mode of interaction between human TRIM69 and Dengue NS2B-NS3 and the subsequent polyubiquitination of the protease by the E3 ligase. We show that NS2B-NS3Δpro is sufficient as a substrate for ubiquitination by TRIM69 using ELISA and in vitro assays. Using hydrogen-deuterium exchange mass spectrometry (HDXMS), we mapped the interface of the interaction between TRIM69 and NS2B-NS3Δpro, and propose a rationale for the binding and subsequent ubiquitination process. Furthermore, through sequence analysis, we showed that the regions targeted by TRIM69 on the DENV-2 NS3 protease (NS3Δpro) are well conserved across DENV serotypes and other flaviviruses, including Zika virus, West Nile virus, and Japanese encephalitis virus. Our results show the direct interactions of TRIM69 with viral proteins, provide mechanistic insights at a molecular level, and highlight the functional relevance of TRIM69 interacting with the Dengue viral protein. Collectively, our findings suggest that TRIM69 may act as a pan-antiflaviviral restriction factor.
(© 2022. The Author(s), under exclusive licence to Springer Nature Switzerland AG.)
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معلومات مُعتمدة: R154-000-C07-114 Ministry of Education (SG); R154-000-697-112 Ministry of Education (SG)
فهرسة مساهمة: Keywords: Antiviral mechanism; Dengue virus; HDXMS; NS2–NS3 protease; TRIM69
المشرفين على المادة: 0 (Tripartite Motif Proteins)
0 (Viral Nonstructural Proteins)
EC 2.3.2.27 (TRIM69 protein, human)
EC 2.3.2.27 (Ubiquitin-Protein Ligases)
EC 3.4.21.- (NS3 protease, dengue virus)
EC 3.4.21.- (Serine Endopeptidases)
تواريخ الأحداث: Date Created: 20220410 Date Completed: 20220412 Latest Revision: 20240516
رمز التحديث: 20240516
مُعرف محوري في PubMed: PMC11072344
DOI: 10.1007/s00018-022-04245-x
PMID: 35397701
قاعدة البيانات: MEDLINE
الوصف
تدمد:1420-9071
DOI:10.1007/s00018-022-04245-x