HIV Assembly, Release and Maturation

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Human Virology and Viral Diseases".

Deadline for manuscript submissions: 30 November 2024 | Viewed by 1153

Special Issue Editor


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Guest Editor
HIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702, USA
Interests: protein biochemistry; virology/HIV; optical spectroscopy; mass spectroscopy; analytical centrifugation

Special Issue Information

Dear Colleagues,

The late stages of the HIV-1 replication cycle—assembly, release, and maturation—have previously defied detailed structural characterization due to the complexity of the multi-scale structural reorganizations involved. Recent progress in cryo-electron microscopy, structural biology, molecular biology, solid-state NMR, and the application of molecular modeling to large systems has now revealed the intricacies of the complex sequence of events that controls these stages. The domain rearrangements that drive global reorganization between the immature and mature states are now being understood at an atomistic level. The mechanisms that determine the selective packaging of genomic RNA into virions are now better understood, as is the importance of inositol hexakisphosphate (IP6) in the generation of both immature Gag and mature capsid lattices. The extent to which flexibility/dynamics play a regulatory role in the maturation process, and the concomitant reorganization of the envelope glycoproteins, is now better appreciated. Research papers exploring the implications of these findings to the replication cycle of HIV-1, drug design, and therapeutic interventions are invited to contribute to this Special Issue. Studies focusing on the virology, cell biology, and biochemistry of these stages are appropriate. Inter-disciplinary studies are also welcome.

Dr. Siddhartha Datta
Guest Editor

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Keywords

  • HIV assembly and maturation
  • capsid stability
  • inositol hexakisphosphate (IP6)
  • genome recognition
  • endogenous reverse transcription
  • reorganization
  • maturation inhibitors
  • flexibility and dynamics

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Published Papers (1 paper)

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Research

19 pages, 3575 KiB  
Article
Putting a Kink in HIV-1 Particle Infectivity: Rocaglamide Inhibits HIV-1 Replication by Altering Gag-Genomic RNA Interaction
by Paul Rosenfeld, Gatikrushna Singh, Amanda Paz Herrera, Juan Ji, Bradley Seufzer, Xiao Heng, Kathleen Boris-Lawrie and Alan Cochrane
Viruses 2024, 16(9), 1506; https://doi.org/10.3390/v16091506 - 23 Sep 2024
Viewed by 700
Abstract
Our examination of RNA helicases for effects on HIV-1 protein production and particle assembly identified Rocaglamide (RocA), a known modulator of eIF4A1 function, as an inhibitor of HIV-1 replication in primary CD4+ T cells and three cell systems. HIV-1 attenuation by low-nM [...] Read more.
Our examination of RNA helicases for effects on HIV-1 protein production and particle assembly identified Rocaglamide (RocA), a known modulator of eIF4A1 function, as an inhibitor of HIV-1 replication in primary CD4+ T cells and three cell systems. HIV-1 attenuation by low-nM RocA doses was associated with reduced viral particle formation without a marked decrease in Gag production. Rather, the co-localization of Gag and HIV-1 genomic RNA (gRNA) assemblies was impaired by RocA treatment in a reversible fashion. Ribonucleoprotein (RNP) immunoprecipitation studies recapitulated the loss of Gag-gRNA assemblies upon RocA treatment. Parallel biophysical studies determined that neither RocA nor eIF4A1 independently affected the ability of Gag to interact with viral RNA, but together, they distorted the structure of the HIV-1 RNP visualized by electron microscopy. Taken together, several lines of evidence indicate that RocA induces stable binding of eIF4A1 onto the viral RNA genome in a manner that interferes with the ordered assembly of Gag along Gag-gRNA assemblies required to generate infectious virions. Full article
(This article belongs to the Special Issue HIV Assembly, Release and Maturation)
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