Viral Condensates and Virus Interference with Host Membraneless Organelles
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Immunology".
Deadline for manuscript submissions: closed (30 June 2023) | Viewed by 10316
Special Issue Editors
Interests: intrinsically disordered proteins; folding copuled to binding; protein-protein interactions; structural transitions; paramyxoviruses
Special Issues, Collections and Topics in MDPI journals
Interests: respiratory syncytial virus; protein-protein interactions; viral factories; nucleoprotein; phosphoprotein
Special Issue Information
Dear Colleagues,
Intrinsically disordered proteins (IDPs) or regions (IDRs) are ubiquitous functional proteins/regions devoid of stable secondary and tertiary structure. Compelling experimental evidence gathered during the last decade points to a critical role for IDPs/IDRs, either alone or in conjunction with nucleic acids, in promoting liquid–liquid phase separation (LLPS). LLPS is a physicochemical process whereby an initially homogenous solution turns into two distinct phases—a “dense” phase that contains the major portion of the dissolved macromolecules, and a “light” phase containing the solvent. LLPS is not merely an in vitro process. Rather, it also occurs in the cellular context, where it drives the formation of so-called membrane-less organelles (MLOs) (e.g., nucleoli, nuclear speckles, Cajal bodies, processing bodies, stress granules, aggresomes, centrosomes, etc). MLOs are supramolecular assemblies possessing regulatory, structural, and enzymatic functions. They are responsible for the spatial and temporal organization of the cell and play a crucial role in a number of physiological processes. Liquid biocondensates resulting from LLPS can also undergo “maturation”, developing into gelled and/or solid-like forms that can eventually nucleate amyloid-like fibrils. Protein aggregation into amyloid fibrils is the archetype of aberrant biomolecular self-assembly processes associated with uncurable neurodegenerative diseases. Likewise, phase transitions from liquid to solid are mostly associated with pathological states.
The phenomenon of LLPS is also exploited by viruses. Viruses take advantage of LLPS for their replication either by interfering with (dis)assembly and regulation of host MLOs or by eliciting the formation of viral factories, i.e., condensates made of their own proteins either alone or in association with nucleic acids. Such viral inclusions are sites where viral replication and assembly take place and where specific viral and cellular proteins, along with nucleic acids, concentrate. They serve as platforms for optimized viral replication and/or assembly via selective uptake or exclusion of specific cellular components and shielding from the host immune defense. So far, the majority of studies have focused on LLPS in relation with replication compartments, and few studies have described interference with host functions. Likewise, only a few studies have focused on the functional impact of phase transitions towards gelled and/or fibrillar states of viral condensates. Examples of fibrils made of viral proteins have just begun to be reported, and the possible implications for pathogenesis are just starting to be discussed.
This Special Issue aims at filling this gap by collecting contributions that cover different aspects of viral condensate formation with an emphasis on new promising antiviral approaches that target these processes.
Dr. Sonia Longhi
Dr. Marie Galloux
Guest Editors
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