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Editorial

Introduction to Special Issue “The 11th International Retroviral Nucleocapsid and Assembly Symposium”

1
Department of Physics, Northeastern University, Boston, MA 02115, USA
2
Department of Microbiology and Immunology, University of Michigan, Ann Arbor, MI 48109, USA
*
Authors to whom correspondence should be addressed.
Submission received: 29 October 2020 / Accepted: 30 October 2020 / Published: 31 October 2020
(This article belongs to the Special Issue The 11th International Retroviral Nucleocapsid and Assembly Symposium)
The 11th International Retroviral Nucleocapsid and Assembly Symposium was held August 15–17, 2019, on the campus of Northeastern University. The meeting consisted of 40 oral presentations and a poster session while providing a stimulating environment to advance our understanding of retroviral assembly and replication and promoting interactions between young scientists and prominent researchers. The presentations covered a range of topics related to retroviral replication and assembly, including biophysical and structural studies, the roles of Gag, NC, RNA, and membranes in retroviral replication and assembly, interactions with cellular factors, virus assembly and budding, and therapeutic strategies. As an outcome of the meeting, this Special Issue was organized. Due to the pandemic, deadlines for the Special Issue were extended, and the issue was completed in October 2020.
The eleven manuscripts published as part of this Special Issue reflect the breadth of topics covered by the symposium, ranging from fundamental biophysical studies of the molecular interactions involved in retroviral replication and assembly to the characterization of complex cellular interactions involved in these processes. Studies of molecular biophysics and biochemistry included a study of the dimerization of the Rous Sarcoma Virus genomic RNA [1], comparison of the nucleic acid chaperone activity and RNA destabilization of HIV-1 Gag and its cleavage product NCp7 [2], and dissection of the contributions of different domains within the HIV-1 Gag polyprotein to specific and nonspecific interactions with RNA [3]. Continuing the theme of critical RNA structural transitions and interactions, another manuscript describes a new approach to the 3D modeling of viral regulatory RNA [4]. These studies shed new light on or describe methods to study critical retroviral replication processes in vitro at the molecular level. Additional studies probed retroviral replication in the context of subcellular structures. They include a study of roles played by an RSV NC basic sequence in RNA nuclear export and packaging specificity [5] and an investigation of a determinant for recruitment of TSG101, a host ESCRT pathway protein, to HIV-1 assembly sites at the plasma membrane [6]. Another study zeroed in on the order and frequency of recruitment of other ESCRT proteins to each single virus assembly site, dissecting the complex molecular mechanism of particle release [7]. Beyond retroviruses, a manuscript describing bioinformatics and meta-analyses conceptualizes how most viruses induce liquid–liquid phase separation to form nucleocapsid protein biomolecular condensates towards virus particle formation [8]. Finally, three review articles cover recent findings on the molecular details of how ESCRT pathway proteins facilitate retroviral particle release [9], lipid- and tRNA-regulated HIV-1 Gag localization to the plasma membrane and its effects on transmembrane protein distribution [10], and the mechanism of membrane microdomain phase separation as determined from live cell imaging of the retroviral assembly process [11]. Overall, these studies demonstrate how interactions between scientists with different areas of expertise lead to the application of new methods, which in turn yields significant new insights into critical processes in retroviral replication and assembly.

Funding

The Symposium was supported in part by the National Institute of Allergy and Infectious Diseases of the National Institutes of Health under Award Number R13AI147353. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

Conflicts of Interest

The authors declare no conflict of interest.

References

  1. Liu, S.; Kaddis Maldonado, R.; Rye-McCurdy, T.; Binkley, C.; Bah, A.; Chen, E.C.; Rice, B.L.; Parent, L.J.; Musier-Forsyth, K. Rous Sarcoma Virus Genomic RNA Dimerization Capability In Vitro Is Not a Prerequisite for Viral Infectivity. Viruses 2020, 12, 568. [Google Scholar] [CrossRef] [PubMed]
  2. McCauley, M.J.; Rouzina, I.; Li, J.; Nunez, M.E.; Williams, M.C. Significant Differences in RNA Structure Destabilization by HIV-1 Gag∆p6 and NCp7 Proteins. Viruses 2020, 12, 484. [Google Scholar] [CrossRef] [PubMed]
  3. Kroupa, T.; Datta, S.A.K.; Rein, A. Distinct Contributions of Different Domains within the HIV-1 Gag Polyprotein to Specific and Nonspecific Interactions with RNA. Viruses 2020, 12, 394. [Google Scholar] [CrossRef] [PubMed] [Green Version]
  4. Osmer, P.S.; Singh, G.; Boris-Lawrie, K. A New Approach to 3D Modeling of Inhomogeneous Populations of Viral Regulatory RNA. Viruses 2020, 12, 1108. [Google Scholar] [CrossRef] [PubMed]
  5. Rice, B.L.; Lochmann, T.L.; Parent, L.J. RNA-Binding Domains of Heterologous Viral Proteins Substituted for Basic Residues in the RSV Gag NC Domain Restore Specific Packaging of Genomic RNA. Viruses 2020, 12, 370. [Google Scholar] [CrossRef] [PubMed] [Green Version]
  6. Watanabe, S.M.; Strickland, M.; Tjandra, N.; Carter, C.A. RNA Binding Suppresses Tsg101 Recognition of Ub-Modified Gag and Facilitates Recruitment to the Plasma Membrane. Viruses 2020, 12, 447. [Google Scholar] [CrossRef] [PubMed] [Green Version]
  7. Gupta, S.; Bendjennat, M.; Saffarian, S. Abrogating ALIX Interactions Results in Stuttering of the ESCRT Machinery. Viruses 2020, 12, 1032. [Google Scholar] [CrossRef] [PubMed]
  8. Monette, A.; Mouland, A.J. Zinc and Copper Ions Differentially Regulate Prion-Like Phase Separation Dynamics of Pan-Virus Nucleocapsid Biomolecular Condensates. Viruses 2020, 12, 1179. [Google Scholar] [CrossRef] [PubMed]
  9. Rose, K.M.; Hirsch, V.M.; Bouamr, F. Budding of a Retrovirus: Some Assemblies Required. Viruses 2020, 12, 1188. [Google Scholar] [CrossRef] [PubMed]
  10. Thornhill, D.; Murakami, T.; Ono, A. Rendezvous at Plasma Membrane: Cellular Lipids and tRNA Set up Sites of HIV-1 Particle Assembly and Incorporation of Host Transmembrane Proteins. Viruses 2020, 12, 842. [Google Scholar] [CrossRef] [PubMed]
  11. Sengupta, P.; Lippincott-Schwartz, J. Revisiting Membrane Microdomains and Phase Separation: A Viral Perspective. Viruses 2020, 12, 745. [Google Scholar] [CrossRef] [PubMed]
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MDPI and ACS Style

Williams, M.C.; Ono, A. Introduction to Special Issue “The 11th International Retroviral Nucleocapsid and Assembly Symposium”. Viruses 2020, 12, 1243. https://0-doi-org.brum.beds.ac.uk/10.3390/v12111243

AMA Style

Williams MC, Ono A. Introduction to Special Issue “The 11th International Retroviral Nucleocapsid and Assembly Symposium”. Viruses. 2020; 12(11):1243. https://0-doi-org.brum.beds.ac.uk/10.3390/v12111243

Chicago/Turabian Style

Williams, Mark C., and Akira Ono. 2020. "Introduction to Special Issue “The 11th International Retroviral Nucleocapsid and Assembly Symposium”" Viruses 12, no. 11: 1243. https://0-doi-org.brum.beds.ac.uk/10.3390/v12111243

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