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The Capsid Protein, a Master Regulator of HIV-1 Replication

Edited by 
Felipe Diaz-Griffero, Albert Einstein College of Medicine, USA

The HIV-1 Core is composed of ~1500 monomers of capsid that are derived from ~2500 Gag precursor molecules to house the dimeric viral RNA genome of HIV-1. Upon viral fusion, the core is released into the cytoplasm where HIV-1 replication begins. The viral life cycle of HIV-1 comprises several steps that are spatially and temporally separated in the cytoplasm and nucleus of the cell; these steps, not in order, are known as uncoating, reverse transcription, nuclear import, integration, expression, particle assembly, particle release and maturation.

Although these steps occur at different times of infection, the capsid protein has emerged as a master regulator for many, if not all, of these steps. In the last 20 years, major evidence has emerged demonstrating that the HIV-1 capsid by itself and/or its ability to interact with celullar host factors is/are necessary for the proper occurrence of uncoating, reverse transcription, nuclear import, integration, particle assembly, particle release and the infection of non-dividing cells.

This thematic series published in Retrovirology contains a collection of reviews highlighting the contribution of capsid and their interactors to each of the different HIV-1 replication steps, with the final goal of generating a comprehensive and educational material with the most up to date information. These reviews will also shed light on the events that are not yet known in HIV-1 replication, which should be considered as the next mile stone by scientists working in this field.    

Submission instructions

Before submitting your manuscript, please ensure you have carefully read the submission guidelines for Retrovirology.

The complete manuscript should be submitted through the journal submission system.

To ensure that you submit to the correct thematic series please select this thematic series in the drop-down menu upon submission.

Deadline for submissions: 31 December 2021

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