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Cells
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Intrinsically Disordered Proteins in Host Function and Subversion by Pathogens
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Intrinsically Disordered Proteins in Host Function and Subversion by Pathogens

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cellular Immunology".

Deadline for manuscript submissions: closed (31 January 2021) | Viewed by 14759

Special Issue Editors

Dr. Natalie Borg

E-Mail Website
Guest Editor
Head, Immunity and Immune Evasion Lab, School of Health and Biomedical Sciences, RMIT University, Bundoora 3083, Australia
Interests: antiviral immunity; infection; nucleocytoplasmic transport; immune evasion host-pathogen interactions
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. David A. Jans

E-Mail Website
Guest Editor
1. Nuclear Signalling Lab, Infection and Immunity Program, Monash Biomedicine Discovery Institute, Clayton, Australia
2. Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
Interests: regulation of nucleocytoplasmic transport; viral infection; stress biology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Many proteins critical to cell function as well as pathogenic conditions are intrinsically disordered proteins (IDPs) or contain intrinsically disordered regions (IDRs). These IDP/IDRs lack persistent structure in solution, and their inherent plasticity enables them to bind to multiple partners. This is integral to host processes such as transport into and out of the nucleus, which in turn is central to cell signalling in innate immune responses. The ability to bind to multiple partners is also key to the strategies pathogens use to circumvent the innate immune response. Clearly, delineating the relationship between IDP/IDR structure and function is central to understanding the host–pathogen interface.
This relationship is complicated, however, by the fact that inherent lack of structure hampers high-resolution structure determination. Innovative approaches are required to give insight into the molecular detail and dynamics of IDPs/IDRs, how this impacts host cell function and how it is exploited by pathogens.
This Special Issue will focus on the basic biology of host- and pathogen-derived IDRs and IDPs, as well as their contribution to innate immunity and infection.

Dr. Natalie Borg
Prof. David A. Jans
Guest Editors

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

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Keywords

  • Intrinsically disordered protein
  • Unstructured proteinsare

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Published Papers (3 papers)

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Review

14 pages, 2442 KiB  
Review
Metal Ions Induce Liquid Condensate Formation by the F Domain of Aedes aegypti Ecdysteroid Receptor. New Perspectives of Nuclear Receptor Studies
by Anna Więch, Aneta Tarczewska, Andrzej Ożyhar and Marek Orłowski
Cells 2021, 10(3), 571; https://doi.org/10.3390/cells10030571 - 5 Mar 2021
Cited by 6 | Viewed by 2814
Abstract
The superfamily of nuclear receptors (NRs), composed of ligand-activated transcription factors, is responsible for gene expression as a reaction to physiological and environmental changes. Transcriptional machinery may require phase separation to fulfil its role. Although NRs have a similar canonical structure, their C-terminal [...] Read more.
The superfamily of nuclear receptors (NRs), composed of ligand-activated transcription factors, is responsible for gene expression as a reaction to physiological and environmental changes. Transcriptional machinery may require phase separation to fulfil its role. Although NRs have a similar canonical structure, their C-terminal domains (F domains) are considered the least conserved and known regions. This article focuses on the peculiar molecular properties of the intrinsically disordered F domain of the ecdysteroid receptor from the Aedes aegypti mosquito (AaFEcR), the vector of the world’s most devastating human diseases such as dengue and Zika. The His-Pro-rich segment of AaFEcR was recently shown to form the unique poly-proline helix II (PPII) in the presence of Cu2+. Here, using widefield microscopy of fluorescently labeled AaFEcR, Zn2+- and Cu2+-induced liquid-liquid phase separation (LLPS) was observed for the first time for the members of NRs. The perspectives of this finding on future research on the F domain are discussed, especially in relation to other NR members. Full article
(This article belongs to the Special Issue Intrinsically Disordered Proteins in Host Function and Subversion by Pathogens)
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Graphical abstract

24 pages, 1759 KiB  
Review
The Role of Protein Disorder in Nuclear Transport and in Its Subversion by Viruses
by Jacinta M. Wubben, Sarah C. Atkinson and Natalie A. Borg
Cells 2020, 9(12), 2654; https://doi.org/10.3390/cells9122654 - 10 Dec 2020
Cited by 20 | Viewed by 7329
Abstract
The transport of host proteins into and out of the nucleus is key to host function. However, nuclear transport is restricted by nuclear pores that perforate the nuclear envelope. Protein intrinsic disorder is an inherent feature of this selective transport barrier and is [...] Read more.
The transport of host proteins into and out of the nucleus is key to host function. However, nuclear transport is restricted by nuclear pores that perforate the nuclear envelope. Protein intrinsic disorder is an inherent feature of this selective transport barrier and is also a feature of the nuclear transport receptors that facilitate the active nuclear transport of cargo, and the nuclear transport signals on the cargo itself. Furthermore, intrinsic disorder is an inherent feature of viral proteins and viral strategies to disrupt host nucleocytoplasmic transport to benefit their replication. In this review, we highlight the role that intrinsic disorder plays in the nuclear transport of host and viral proteins. We also describe viral subversion mechanisms of the host nuclear transport machinery in which intrinsic disorder is a feature. Finally, we discuss nuclear import and export as therapeutic targets for viral infectious disease. Full article
(This article belongs to the Special Issue Intrinsically Disordered Proteins in Host Function and Subversion by Pathogens)
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16 pages, 2592 KiB  
Review
The Intrinsically Disordered W Protein Is Multifunctional during Henipavirus Infection, Disrupting Host Signalling Pathways and Nuclear Import
by Sofiya Tsimbalyuk, Emily M. Cross, Mikayla Hoad, Camilla M. Donnelly, Justin A. Roby and Jade K. Forwood
Cells 2020, 9(8), 1913; https://doi.org/10.3390/cells9081913 - 18 Aug 2020
Cited by 12 | Viewed by 3792 | Correction
Abstract
Nipah and Hendra viruses are highly pathogenic, zoonotic henipaviruses that encode proteins that inhibit the host’s innate immune response. The W protein is one of four products encoded from the P gene and binds a number of host proteins to regulate signalling pathways. [...] Read more.
Nipah and Hendra viruses are highly pathogenic, zoonotic henipaviruses that encode proteins that inhibit the host’s innate immune response. The W protein is one of four products encoded from the P gene and binds a number of host proteins to regulate signalling pathways. The W protein is intrinsically disordered, a structural attribute that contributes to its diverse host protein interactions. Here, we review the role of W in innate immune suppression through inhibition of both pattern recognition receptor (PRR) pathways and interferon (IFN)-responsive signalling. PRR stimulation leading to activation of IRF-3 and IFN release is blocked by henipavirus W, and unphosphorylated STAT proteins are sequestered within the nucleus of host cells by W, thereby inhibiting the induction of IFN stimulated genes. We examine the critical role of nuclear transport in multiple functions of W and how specific binding of importin-alpha (Impα) isoforms, and the 14-3-3 group of regulatory proteins suggests further modulation of these processes. Overall, the disordered nature and multiple functions of W warrant further investigation to understand henipavirus pathogenesis and may reveal insights aiding the development of novel therapeutics. Full article
(This article belongs to the Special Issue Intrinsically Disordered Proteins in Host Function and Subversion by Pathogens)
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