Analysis of LLPS in Herpesvirus Infection
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Analysis of LLPS in Herpesvirus Infection

Herpes virus infections are a group of viral infections caused by different types of herpes viruses. Of the more than 100 known herpesviruses, eight usually infect only humans, including herpes simplex virus type 1 (HSV-1), herpes simplex virus type 2 (HSV-2), varicella-zoster virus (VZV), EB virus (EBV), cytomegalovirus (CMV), and human herpesviruses 6, 7, and 8 (HHV-6, HHV-7, and HHV-8). Herpesvirus are highly infectious and can be transmitted through direct contact with an infected person. Herpesvirus can be classified into three subfamilies (α, β and γ) based on genomic organization and pathogenesis. Studies have shown that liquid-liquid phase separation (LLPS ) mediates some biomolecular condensates as replication compartments or inclusion bodies in herpesvirus, such as UL112-113 protein and ICP4 protein.

Herpesvirus tegument protein ORF52 undergoes LLPS to form cytoplasmic virion assembly compartments.Fig. 1. Herpesvirus tegument protein ORF52 undergoes LLPS to form cytoplasmic virion assembly compartments. (Chung W C, et al., 2022)

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All three subfamilies of herpesvirus are shown to form cytoplasmic virosome assembly chambers. Studying LLPS in herpesvirus infection is currently an active area of research, and its exact mechanism and functional significance are not fully understood. Our laboratory has advanced circular dichroism, limited protein hydrolysis, small angle ray scattering and optical microscopy to characterize the structure and LLPS properties of several herpesvirus proteins, including ICP27, ICP4, ICP8, ORF33, ORF45, ORF52, and UL112-113, etc. CD BioSciences provides professional services to analyze the formation and role of LLPS in herpesvirus replication, capsid assembly, progeny export and antiviral immunomodulation. We aim to develop a promising therapeutic strategy for herpesvirus infections.

Herpesvirus assembly obtains the most epithelial proteins and envelopes occurring in the cytoplasmic virosome assembly compartment. Our technical team is dedicated to constructing recombinant herpesviruses expressing fluorescently labeled cortical proteins to help our clients analyze in detail the formation of cytoplasmic virosome assembly compartments of three subtypes of herpesviruses, including:

  • Analyzing the formation and spatio-temporal variation of cytoplasmic virosome assembly compartments in living cells.
  • In vitro and in vivo assays of conditions that promote the cortical protein LLPS.

Importantly, our technical team is developing recombinant vaccines based on herpesvirus phase separation proteins for antiviral immunization and investigating antiviral strategies that allow herpesvirus phase separation proteins to be used as potential drug targets.

Combining sensitive live imaging and correlated photosynthetic electron microscopy (CLEM) techniques with a variety of recombinant viruses, we can comprehensively study the biophysical properties of herpesvirus cytoplasmic virosome assembly chambers by LLPS, not only in transfection or in vitro analysis systems, but also in the context of viral infection. In addition, we are developing a novel and effective anti-herpesvirus strategy targeting LLPS. Our services are widely used in preclinical research on herpesvirus infection biology, diagnosis and treatment. If you are interested in our services, please feel free to contact us.

Reference

  1. Chung W C, Ahn J H, Song M J. (2022) Liquid-liquid phase separation drives herpesvirus assembly in the cytoplasm[J]. The Journal of Cell Biology. 222(1): e202211015-e202211015.
For research use only, not intended for any clinical use.
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