دورية أكاديمية
Herpes simplex virus type-1 cVAC formation in neuronal cells is mediated by dynein motor function and glycoprotein retrieval from the plasma membrane.
| العنوان: | Herpes simplex virus type-1 cVAC formation in neuronal cells is mediated by dynein motor function and glycoprotein retrieval from the plasma membrane. |
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| المؤلفون: | White S; Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, USA., Roller R; Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, USA. |
| المصدر: | Journal of virology [J Virol] 2024 Jul 23; Vol. 98 (7), pp. e0071324. Date of Electronic Publication: 2024 Jun 20. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Society For Microbiology Country of Publication: United States NLM ID: 0113724 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1098-5514 (Electronic) Linking ISSN: 0022538X NLM ISO Abbreviation: J Virol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Washington Dc : American Society For Microbiology Original Publication: Baltimore, American Society for Microbiology. |
| مواضيع طبية MeSH: | Herpesvirus 1, Human*/physiology , Herpesvirus 1, Human*/metabolism , Dyneins*/metabolism , Cell Membrane*/metabolism , Cell Membrane*/virology , Neurons*/virology , Neurons*/metabolism , Dynactin Complex*/metabolism , Viral Envelope Proteins*/metabolism , Microtubule-Associated Proteins*/metabolism , Virus Assembly*, Humans ; Cell Line ; Animals ; Viral Replication Compartments/metabolism ; Microtubules/metabolism |
| مستخلص: | Herpesvirus assembly requires the cytoplasmic association of large macromolecular and membrane structures that derive from both the nucleus and cytoplasmic membrane systems. Results from the study of human cytomegalovirus (HCMV) in cells where it organizes a perinuclear cytoplasmic virus assembly compartment (cVAC) show a clear requirement for the minus-end-directed microtubule motor, dynein, for virus assembly. In contrast, the assembly of herpes simplex virus -1 (HSV-1) in epithelial cells where it forms multiple dispersed, peripheral assembly sites is only mildly inhibited by the microtubule-depolymerizing agent, nocodazole. Here, we make use of a neuronal cell line system in which HSV-1 forms a single cVAC and show that dynein and its co-factor dynactin localize to the cVAC, and dynactin is associated with membranes that contain the virion tegument protein pUL11. We also show that the virus membrane-associated structural proteins pUL51 and the viral envelope glycoprotein gE arrive at the cVAC by different routes. Specifically, gE arrives at the cVAC after retrieval from the plasma membrane, suggesting the need for an intact retrograde transport system. Finally, we demonstrate that inhibition of dynactin function profoundly inhibits cVAC formation and virus production during the cytoplasmic assembly phase of infection.IMPORTANCEMany viruses reorganize cytoplasmic membrane systems and macromolecular transport systems to promote the production of progeny virions. Clarifying the mechanisms by which they accomplish this may reveal novel therapeutic strategies and illustrate mechanisms that are critical for normal cellular organization. Here, we explore the mechanism by which HSV-1 moves macromolecular and membrane cargo to generate a virus assembly compartment in the infected cell. We find that the virus makes use of a well-characterized, microtubule-based transport system that is stabilized against drugs that disrupt microtubules. Competing Interests: The authors declare no conflict of interest. |
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| معلومات مُعتمدة: | T32 AI007061 United States AI NIAID NIH HHS; R01 AI150718 United States AI NIAID NIH HHS; R21 AI153683 United States AI NIAID NIH HHS; University of Iowa Graduate College; R01AI150718 HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID); R21AI153683 HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID); T32AI007061 HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) |
| فهرسة مساهمة: | Keywords: dynactin; dynein; envelopment; herpes simplex; plasma membrane retrieval; virion assembly |
| المشرفين على المادة: | EC 3.6.4.2 (Dyneins) 0 (Dynactin Complex) 0 (Viral Envelope Proteins) 0 (Microtubule-Associated Proteins) 0 (glycoprotein E, herpes simplex virus type 1) |
| تواريخ الأحداث: | Date Created: 20240620 Date Completed: 20240723 Latest Revision: 20240725 |
| رمز التحديث: | 20240726 |
| مُعرف محوري في PubMed: | PMC11265375 |
| DOI: | 10.1128/jvi.00713-24 |
| PMID: | 38899931 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1098-5514 |
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| DOI: | 10.1128/jvi.00713-24 |