Academic Journal
A Conserved Leucine Zipper Motif in Gammaherpesvirus ORF52 Is Critical for Distinct Microtubule Rearrangements
| العنوان: | A Conserved Leucine Zipper Motif in Gammaherpesvirus ORF52 Is Critical for Distinct Microtubule Rearrangements |
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| المؤلفون: | Loftus, Matthew S., Verville, Nancy, Kedes, Dean H. |
| المساهمون: | Frueh, Klaus, HHS | NIH | National Cancer Institute, HHS | NIH | National Institute of Dental and Craniofacial Research, University of Virginia |
| المصدر: | Journal of Virology ; volume 91, issue 17 ; ISSN 0022-538X 1098-5514 |
| بيانات النشر: | American Society for Microbiology |
| سنة النشر: | 2017 |
| الوصف: | Productive viral infection often depends on the manipulation of the cytoskeleton. Herpesviruses, including rhesus monkey rhadinovirus (RRV) and its close homolog, the oncogenic human gammaherpesvirus Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 (KSHV/HHV8), exploit microtubule (MT)-based retrograde transport to deliver their genomes to the nucleus. Subsequently, during the lytic phase of the life cycle, the maturing viral particles undergo orchestrated translocation to specialized regions within the cytoplasm, leading to tegumentation, secondary envelopment, and then egress. As a result, we hypothesized that RRV might induce changes in the cytoskeleton at both early and late stages of infection. Using confocal imaging, we found that RRV infection led to the thickening and acetylation of MTs emanating from the MT-organizing center (MTOC) shortly after viral entry and more pronounced and diffuse MT reorganization during peak stages of lytic gene expression and virion production. We subsequently identified open reading frame 52 (ORF52), a multifunctional and abundant tegument protein, as being the only virally encoded component responsible for these cytoskeletal changes. Mutational and modeling analyses indicated that an evolutionarily conserved, truncated leucine zipper motif near the N terminus as well as a strictly conserved arginine residue toward the C terminus of ORF52 play critical roles in its ability to rearrange the architecture of the MT cytoskeleton. Taken together, our findings combined with data from previous studies describing diverse roles for ORF52 suggest that it likely binds to different cellular components, thereby allowing context-dependent modulation of function. IMPORTANCE A thorough understanding of the processes governing viral infection includes knowledge of how viruses manipulate their intracellular milieu, including the cytoskeleton. Altering the dynamics of actin or MT polymerization, for example, is a common strategy employed by viruses to ensure efficient ... |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| DOI: | 10.1128/jvi.00304-17 |
| DOI: | 10.1128/JVI.00304-17 |
| الاتاحة: | http://dx.doi.org/10.1128/jvi.00304-17 https://journals.asm.org/doi/pdf/10.1128/JVI.00304-17 |
| Rights: | https://creativecommons.org/licenses/by/4.0/ ; https://journals.asm.org/non-commercial-tdm-license |
| رقم الانضمام: | edsbas.A64D83F4 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1128/jvi.00304-17 |
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