Special Issue "Retroviral Nucleocapsid Proteins"

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Animal Viruses".

Deadline for manuscript submissions: closed (15 October 2021).

Special Issue Editor

Dr. Olivier Mauffret
Guest Editor
Laboratory of Biology and Applied Pharmacology (LBPA), École Normale Supérieure Paris-Saclay, Université Paris-Saclay, CNRS, UMR 8113, Institut D'Alembert, F-91190 Gif Sur Yvette, France
Interests: viral nucleocapsids, structural biology

Special Issue Information

Dear Colleagues,

Retroviral nucleocapsid (NC) proteins play a key role in retrovirus replication. These proteins, all equipped with one or two CCHC domains able to bind zinc atoms, are endowed with a strong ability to interact with nucleic acids and to reorganize their structure-classifying NCs as nucleic acid chaperones. A striking feature of these proteins is their involvement in several distinct processes of the replication cycle. Like other viral nucleocapsids, retroviral NCs are characterized by their role in the compaction and protection of viral genomes, as well as in the process of particle assembly. In particular, retroviral NCs have been shown to be critically involved in the selection of RNA molecules that will be packaged in the retroviral particle. In addition to these functions, which, historically, were the first to be known and studied, the protein, in its fully matured form, has been revealed to have a crucial function in reverse transcription (RT) processes, the very specific hallmark of retroviruses. Indeed, NC proteins have been shown to be involved in the initiation of RT, in the strand transfer processes, either the obligatory or internal transfers. Due to their involvement in these processes, NC proteins have a crucial role in the ability of retroviral genomes to rapidly evolve and to bypass immunogenic reactions and antiviral therapies.

In this Special Issue of Viruses we aim for research and review papers that explore the numerous and various aspects of the molecular mechanisms related to the functioning of these pleiotropic proteins.

Dr. Olivier Mauffret
Guest Editor

Manuscript Submission Information

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2200 CHF (Swiss Francs). 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.


  • selective RNA packaging
  • genomic RNA
  • retroviruses
  • HIV
  • reverse transcription
  • strand transfers
  • recombination
  • chaperon proteins
  • disordered proteins
  • zinc fingers

Published Papers (1 paper)

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The Zinc Content of HIV-1 NCp7 Affects Its Selectivity for Packaging Signal and Affinity for Stem-Loop 3
Viruses 2021, 13(10), 1922; https://0-doi-org.brum.beds.ac.uk/10.3390/v13101922 - 24 Sep 2021
Viewed by 393
The nucleocapsid (NC) protein of human immunodeficiency (HIV) is a small, highly basic protein containing two CCHC zinc-finger motifs, which is cleaved from the NC domain of the Gag polyprotein during virus maturation. We previously reported that recombinant HIV-1 Gag and NCp7 overexpressed [...] Read more.
The nucleocapsid (NC) protein of human immunodeficiency (HIV) is a small, highly basic protein containing two CCHC zinc-finger motifs, which is cleaved from the NC domain of the Gag polyprotein during virus maturation. We previously reported that recombinant HIV-1 Gag and NCp7 overexpressed in an E. coli host contains two and one zinc ions, respectively, and Gag exhibited much higher selectivity for packaging signal (Psi) and affinity for the stem-loop (SL)-3 of Psi than NCp7. In this study, we prepared NCp7 containing 0 (0NCp7), 1 (NCp7) or 2 (2NCp7) zinc ions, and compared their secondary structure, Psi-selectivity and SL3-affinity. Along with the decrease of the zinc content, less ordered conformations were detected. Compared to NCp7, 2NCp7 exhibited a much higher Psi-selectivity and SL3-affinity, similar to Gag, whereas 0NCp7 exhibited a lower Psi-selectivity and SL3-affinity, similar to the H23&H44K double mutant of NCp7, indicating that the different RNA-binding property of Gag NC domain and the mature NCp7 may be resulted, at least partially, from their different zinc content. This study will be helpful to elucidate the critical roles that zinc played in the viral life cycle, and benefit further investigations of the functional switch from the NC domain of Gag to the mature NCp7. Full article
(This article belongs to the Special Issue Retroviral Nucleocapsid Proteins)
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