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Advances in Structure–Function Investigations of Viruses

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: 25 May 2024 | Viewed by 872

Special Issue Editor

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Guest Editor
Department of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA
Interests: structural biology; 3D image reconstruction; microscopy; vaccine design; virus structures; molecular medicine; genomics; proteomics; metabolomics
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Special Issue Information

Dear Colleagues,

The current wealth of knowledge on high-resolution complex structures makes this an appropriate time to summarize the state of the art in structural dynamics of living architectures. This Special Issue, “Advances in Structure–Function Investigations of Viruses”, includes case studies aiming to reflect highly coherent interplays between macromolecular structures and evolved functions illuminated by studies of microscopy, crystallography, spectroscopy, and computer modeling. This Special Issue will provide biologists with a broad forum to exchange structural descriptors of fascinating virus systems for brainstorming novel solutions in biomedicine collectively in one volume.

Modern molecular and cellular biology instrumentation provides a potent array of wave packets to image, detect, and manipulate major dynamics of macromolecular and subviral assemblies as in the host cellular context. The folding of a polypeptide chain creates local environments from which “activity” can emerge. In the same way, the assembly of large molecular complexes creates dynamic features that would only be feasible in a large construct. The biological implications of such adaptation are explored as it applies to static quasi-symmetry situations and the dynamics of structural transitions. Consequently, virus infections involve the utilization of large macromolecular assemblies as a dynamic consequence of cooperativity and metastability. The compilation and integration of the methodology provide time-resolved observations on the reactivity of structures from near-atomic resolution to various molecular or cellular levels of descriptors. This Special Issue welcomes exploration of extended themes in intracellular networking/compartmentation utilized in the cell entry and replication cycles by various viruses.

With contributions by leading scientists in the field like you, this crucially timed Special Issue presents cutting-edge knowledge in the various fields of structural proteomics of substantial molecular assemblies, focusing on their mechanisms of action. This Special Issue will provide updates on concurrent research to further aid in solving epidemics and designing innovative nanomaterials for the 21st century.

Prof. Dr. R. Holland Cheng
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


  • structure
  • assembly
  • viruses
  • crystallography
  • spectroscopy
  • computer modeling

Published Papers (1 paper)

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12 pages, 5387 KiB  
The Nuclear Localization Signal of Porcine Circovirus Type 4 Affects the Subcellular Localization of the Virus Capsid and the Production of Virus-like Particles
by Jiawei Zheng, Nan Li, Xue Li, Yaqi Han, Xinru Lv, Huimin Zhang and Linzhu Ren
Int. J. Mol. Sci. 2024, 25(5), 2459; https://doi.org/10.3390/ijms25052459 - 20 Feb 2024
Viewed by 629
Porcine circovirus 4 (PCV4) is a newly identified virus belonging to PCV of the Circoviridae family, the Circovirus genus. We previously found that PCV4 is pathogenic in vitro, while the virus’s replication in cells is still unknown. In this study, we evaluated the [...] Read more.
Porcine circovirus 4 (PCV4) is a newly identified virus belonging to PCV of the Circoviridae family, the Circovirus genus. We previously found that PCV4 is pathogenic in vitro, while the virus’s replication in cells is still unknown. In this study, we evaluated the N-terminal of the PCV4 capsid (Cap) and identified an NLS at amino acid residues 4–37 of the N-terminus of the PCV4 Cap, 4RSRYSRRRRNRRNQRRRGLWPRASRRRYRWRRKN37. The NLS was further divided into two fragments (NLS-A and NLS-B) based on the predicted structure, including two α-helixes, which were located at 4RSRYSRRRRNRRNQRR19 and 24PRASRRRYRWRRK36, respectively. Further studies showed that the NLS, especially the first α-helixes formed by the NLS-A fragment, determined the nuclear localization of the Cap protein, and the amino acid 4RSRY7 in the NLS of the PCV4 Cap was the critical motif affecting the VLP packaging. These results will provide a theoretical basis for elucidating the infection mechanism of PCV4 and developing subunit vaccines based on VLPs. Full article
(This article belongs to the Special Issue Advances in Structure–Function Investigations of Viruses)
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