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Chandipura Virus Forms Cytoplasmic Inclusion Bodies through Phase Separation and Proviral Association of Cellular Protein Kinase R and Stress Granule Protein TIA-1.

التفاصيل البيبلوغرافية
العنوان: Chandipura Virus Forms Cytoplasmic Inclusion Bodies through Phase Separation and Proviral Association of Cellular Protein Kinase R and Stress Granule Protein TIA-1.
المؤلفون: Sarkar S; Department of Molecular Medicine, School of Interdisciplinary Studies, Jamia Hamdard University, Hamdard Nagar, New Delhi 110062, India., Ganguly S; Department of Molecular Medicine, School of Interdisciplinary Studies, Jamia Hamdard University, Hamdard Nagar, New Delhi 110062, India., Ganguly NK; Department of Education and Research, AERF, Artemis Hospitals, Gurugram 122001, India., Sarkar DP; Department of Biochemistry, University of Delhi South Campus, New Delhi 110021, India., Sharma NR; Department of Molecular Medicine, School of Interdisciplinary Studies, Jamia Hamdard University, Hamdard Nagar, New Delhi 110062, India.; Department of Education and Research, AERF, Artemis Hospitals, Gurugram 122001, India.
المصدر: Viruses [Viruses] 2024 Jun 26; Vol. 16 (7). Date of Electronic Publication: 2024 Jun 26.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101509722 Publication Model: Electronic Cited Medium: Internet ISSN: 1999-4915 (Electronic) Linking ISSN: 19994915 NLM ISO Abbreviation: Viruses Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI
مواضيع طبية MeSH: eIF-2 Kinase*/metabolism , eIF-2 Kinase*/genetics , T-Cell Intracellular Antigen-1*/metabolism , T-Cell Intracellular Antigen-1*/genetics , Virus Replication* , Inclusion Bodies, Viral*/metabolism, Animals ; Chlorocebus aethiops ; Vero Cells ; Humans ; Stress Granules/metabolism ; Inclusion Bodies/metabolism ; Host-Pathogen Interactions ; Cytoplasmic Granules/metabolism ; Viral Proteins/metabolism ; Viral Proteins/genetics ; Phase Separation
مستخلص: Negative-strand RNA viruses form cytoplasmic inclusion bodies (IBs) representing virus replication foci through phase separation or biomolecular condensation of viral and cellular proteins, as a hallmark of their infection. Alternatively, mammalian cells form stalled mRNA containing antiviral stress granules (SGs), as a consequence of phosphorylation of eukaryotic initiation factor 2α (eIF2α) through condensation of several RNA-binding proteins including TIA-1. Whether and how Chandipura virus (CHPV), an emerging human pathogen causing influenza-like illness, coma and death, forms IBs and evades antiviral SGs remain unknown. By confocal imaging on CHPV-infected Vero-E6 cells, we found that CHPV infection does not induce formation of distinct canonical SGs. Instead, CHPV proteins condense and co-localize together with SG proteins to form heterogeneous IBs, which ensued independent of the activation of eIF2α and eIF2α kinase, protein kinase R (PKR). Interestingly, siRNA-mediated depletion of PKR or TIA-1 significantly decreased viral transcription and virion production. Moreover, CHPV infection also caused condensation and recruitment of PKR to IBs. Compared to SGs, IBs exhibited significant rapidity in disassembly dynamics. Altogether, our study demonstrating that CHPV replication co-optimizes with SG proteins and revealing an unprecedented proviral role of TIA-1/PKR may have implications in understanding the mechanisms regulating CHPV-IB formation and designing antiviral therapeutics. Importance: CHPV is an emerging tropical pathogen reported to cause acute influenza-like illness and encephalitis in children with a very high mortality rate of ~70%. Lack of vaccines and an effective therapy against CHPV makes it a potent pathogen for causing an epidemic in tropical parts of globe. Given these forewarnings, it is of paramount importance that CHPV biology must be understood comprehensively. Targeting of host factors offers several advantages over targeting the viral components due to the generally higher mutation rate in the viral genome. In this study, we aimed at understanding the role of SGs forming cellular RNA-binding proteins in CHPV replication. Our study helps understand participation of cellular factors in CHPV replication and could help develop effective therapeutics against the virus.
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معلومات مُعتمدة: BT/RLF/Re-entry/40/2018 Department of Biotechnology
فهرسة مساهمة: Keywords: Chandipura virus; inclusion bodies; phase separation; protein kinase R; stress granules
المشرفين على المادة: EC 2.7.11.1 (eIF-2 Kinase)
0 (T-Cell Intracellular Antigen-1)
0 (TIA1 protein, human)
0 (Viral Proteins)
تواريخ الأحداث: Date Created: 20240727 Date Completed: 20240727 Latest Revision: 20240729
رمز التحديث: 20240729
مُعرف محوري في PubMed: PMC11281494
DOI: 10.3390/v16071027
PMID: 39066190
قاعدة البيانات: MEDLINE
الوصف
تدمد:1999-4915
DOI:10.3390/v16071027